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*** HYDROLASE 02-JUN-04 1W08 ***elNémo ID: 2407290648031925900Job options:ID = 2407290648031925900 JOBID = HYDROLASE 02-JUN-04 1W08 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE 02-JUN-04 1W08 TITLE STRUCTURE OF T70N HUMAN LYSOZYME COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOZYME; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 19-148; COMPND 5 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C; COMPND 6 EC: 3.2.1.17; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS 115 KEYWDS HYDROLASE, O-GLYCOSYL, HUMAN LYSOZYME, ENZYME, AMYLOID EXPDTA X-RAY DIFFRACTION AUTHOR R.JOHNSON,J.CHRISTODOULOU,B.LUISI,M.DUMOULIN,G.CADDY,M.ALCOCER, AUTHOR 2 G.MURTAGH,D.B.ARCHER,C.M.DOBSON REVDAT 6 13-DEC-23 1W08 1 REMARK REVDAT 5 08-MAY-19 1W08 1 REMARK REVDAT 4 06-MAR-19 1W08 1 REMARK REVDAT 3 24-FEB-09 1W08 1 VERSN REVDAT 2 20-DEC-06 1W08 1 JRNL REVDAT 1 10-JUN-04 1W08 0 JRNL AUTH R.JOHNSON,J.CHRISTODOULOU,M.DUMOULIN,G.CADDY,M.ALCOCER, JRNL AUTH 2 G.MURTAGH,J.R.KUMITA,G.LARSSON,C.V.ROBINSON,D.B.ARCHER, JRNL AUTH 3 B.LUISI,C.M.DOBSON JRNL TITL RATIONALISING LYSOZYME AMYLOIDOSIS: INSIGHTS FROM THE JRNL TITL 2 STRUCTURE AND SOLUTION DYNAMICS OF T70N LYSOZYME. JRNL REF J.MOL.BIOL. V. 352 823 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 16126226 JRNL DOI 10.1016/J.JMB.2005.07.040 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 3529 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200 REMARK 3 FREE R VALUE TEST SET COUNT : 358 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1030 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 88 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.66 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : 0.59000 REMARK 3 B33 (A**2) : -0.65000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.399 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.332 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.331 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS ADDED IN RIDING POSITIONS. REMARK 4 REMARK 4 1W08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1290015270. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-NOV-04 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : OSMIC MIRROR REMARK 200 OPTICS : OSMIC MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3903 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : 0.07500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.14600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 6.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1JSF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP METHOD AT 293K. DROPLET REMARK 280 RESERVOIR SOLUTION MIXED 1:1 WITH 10 MG/ML PROTEIN, 10 MM HEPES REMARK 280 BUFFER PH 7.5, 0.4 M LICL. RESERVOIR 2.5 M NACL, 20 MM NAOAC PH REMARK 280 4.5., PH 4.50, VAPOR DIFFUSION, HANGING DROP REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 15.55850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.24400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.08900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.24400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 15.55850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.08900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O GLY A 37 NE2 GLN A 126 4566 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ASP A 49 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP A 53 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES REMARK 500 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES REMARK 500 ASP A 67 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 GLN A 86 CA - CB - CG ANGL. DEV. = 13.8 DEGREES REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES REMARK 500 ARG A 101 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG A 119 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 38 31.63 76.05 REMARK 500 GLN A 58 56.52 35.48 REMARK 500 LYS A 69 -76.45 -91.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1131 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 133L RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ARG 115 REPLACED BY HIS (R115H) REMARK 900 RELATED ID: 134L RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ARG 115 REPLACED BY GLU (R115E) REMARK 900 RELATED ID: 1B5U RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANT REMARK 900 RELATED ID: 1B5V RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANTS REMARK 900 RELATED ID: 1B5W RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANTS REMARK 900 RELATED ID: 1B5X RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANTS REMARK 900 RELATED ID: 1B5Y RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANTS REMARK 900 RELATED ID: 1B5Z RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER ->ALA REMARK 900 MUTANTS REMARK 900 RELATED ID: 1B7L RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7M RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7N RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7O RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7P RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7Q RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7R RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1B7S RELATED DB: PDB REMARK 900 VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES REMARK 900 RELATED ID: 1BB3 RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT A96L REMARK 900 RELATED ID: 1BB4 RELATED DB: PDB REMARK 900 HUMAN LYSOZYME DOUBLE MUTANT A96L, W109H REMARK 900 RELATED ID: 1BB5 RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT A96L COMPLEXED WITH CHITOTRIOSE REMARK 900 RELATED ID: 1C43 RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME WITH FOREIGN N- TERMINAL RESIDUES REMARK 900 RELATED ID: 1C45 RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME WITH FOREIGN N- TERMINAL RESIDUES REMARK 900 RELATED ID: 1C46 RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME WITH FOREIGN N- TERMINAL RESIDUES REMARK 900 RELATED ID: 1C7P RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES REMARK 900 (EAEA) AT THE N- TERMINAL REMARK 900 RELATED ID: 1CJ6 RELATED DB: PDB REMARK 900 T11A MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CJ7 RELATED DB: PDB REMARK 900 T11V MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CJ8 RELATED DB: PDB REMARK 900 T40A MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CJ9 RELATED DB: PDB REMARK 900 T40V MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CKC RELATED DB: PDB REMARK 900 T43A MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CKD RELATED DB: PDB REMARK 900 T43V MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CKF RELATED DB: PDB REMARK 900 T52A MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CKG RELATED DB: PDB REMARK 900 T52V MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1CKH RELATED DB: PDB REMARK 900 T70V MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1D6P RELATED DB: PDB REMARK 900 HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2', 3'-EPOXYPROPYL N, N'- REMARK 900 DIACETYLCHITOBIOSE REMARK 900 RELATED ID: 1D6Q RELATED DB: PDB REMARK 900 HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2', 3'-EPOXYPROPYL REMARK 900 GLYCOSIDE OF N- ACETYLLACTOSAMINE REMARK 900 RELATED ID: 1DI3 RELATED DB: PDB REMARK 900 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL REMARK 900 STABILITY AND FOLDING OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1DI4 RELATED DB: PDB REMARK 900 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL REMARK 900 STABILITY AND FOLDING OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1DI5 RELATED DB: PDB REMARK 900 ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL REMARK 900 STABILITY AND FOLDING OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1EQ4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1EQ5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1EQE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1GAY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GAZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GB9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GBO RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GBW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GBX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GBY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GBZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GDW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GDX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GE0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GE1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GE2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GE3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GE4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATLEFT- REMARK 900 HANDED HELICAL POSITIONS REMARK 900 RELATED ID: 1GEV RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GEZ RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF0 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF3 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF4 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF5 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF6 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF7 RELATED DB: PDB REMARK 900 BURIED POLAR MUTANT HUMAN LYSOZYME REMARK 900 RELATED ID: 1GF8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GF9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFG RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFJ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1GFV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1HNL RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH CYS 77 REPLACED BY ALA (C77A) COMPLEXED WITH REMARK 900 GLUTATHIONE REMARK 900 RELATED ID: 1I1Z RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME (Q86D) REMARK 900 RELATED ID: 1I20 RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME (A92D) REMARK 900 RELATED ID: 1I22 RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D) REMARK 900 RELATED ID: 1INU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED ATTHE REMARK 900 SURFACE POSITIONS REMARK 900 RELATED ID: 1IOC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T REMARK 900 RELATED ID: 1IP1 RELATED DB: PDB REMARK 900 G37A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP2 RELATED DB: PDB REMARK 900 G48A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP3 RELATED DB: PDB REMARK 900 G68A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP4 RELATED DB: PDB REMARK 900 G72A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP5 RELATED DB: PDB REMARK 900 G105A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP6 RELATED DB: PDB REMARK 900 G127A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IP7 RELATED DB: PDB REMARK 900 G129A HUMAN LYSOZYME REMARK 900 RELATED ID: 1IWT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 113K. REMARK 900 RELATED ID: 1IWU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 127K. REMARK 900 RELATED ID: 1IWV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 147K. REMARK 900 RELATED ID: 1IWW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 152K. REMARK 900 RELATED ID: 1IWX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 161K. REMARK 900 RELATED ID: 1IWY RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 170K. REMARK 900 RELATED ID: 1IWZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HUMAN LYSOZYME AT 178K. REMARK 900 RELATED ID: 1IX0 RELATED DB: PDB REMARK 900 I59A-3SS HUMAN LYSOZYME REMARK 900 RELATED ID: 1IY3 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE HUMAN LYSOZYME AT 4 DEGREE C REMARK 900 RELATED ID: 1IY4 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE HUMAN LYSOZYME AT 35 DEGREE C REMARK 900 RELATED ID: 1JKA RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP REMARK 900 RELATED ID: 1JKB RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA REMARK 900 RELATED ID: 1JKC RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE REMARK 900 RELATED ID: 1JKD RELATED DB: PDB REMARK 900 HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA REMARK 900 RELATED ID: 1JSF RELATED DB: PDB REMARK 900 FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1JWR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN LYSOZYME AT 100K REMARK 900 RELATED ID: 1LAA RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ASP 53 REPLACED BY GLU (D53E) REMARK 900 RELATED ID: 1LHH RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH VAL 110 REPLACED BY PRO (V110P) REMARK 900 RELATED ID: 1LHI RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH PRO 71 REPLACED BY GLY (P71G) REMARK 900 RELATED ID: 1LHJ RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH PRO 103 REPLACED BY GLY (P103G) REMARK 900 RELATED ID: 1LHK RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ASP 91 REPLACED BY PRO (D91P) REMARK 900 RELATED ID: 1LHL RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH ALA 47 REPLACED BY PROLINE (A47P) REMARK 900 RELATED ID: 1LHM RELATED DB: PDB REMARK 900 LYSOZYME (MUTANT WITH CYS 77 REPLACED BY ALA AND CYS 95 REPLACED BY REMARK 900 ALA) (C77A, C95A) REMARK 900 RELATED ID: 1LMT RELATED DB: PDB REMARK 900 LYSOZYME (LZ_CRGD4) MUTANT WITH CYS-ARG-GLY -ASP-SER-CYS INSERTED REMARK 900 BETWEEN VAL 74 AND ASN 75 (INS(74-CRFDSC-75) COMPLEXED WITH TRI- REMARK 900 ACETYL-CHITOTRIOSE REMARK 900 RELATED ID: 1LOZ RELATED DB: PDB REMARK 900 AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1LYY RELATED DB: PDB REMARK 900 AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME REMARK 900 RELATED ID: 1LZ1 RELATED DB: PDB REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1LZ4 RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH CYS 77 REPLACED BY ALA (C77A) REMARK 900 RELATED ID: 1LZ5 RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH FOUR AMINO ACID RESIDUES (ARG 74A, GLY 74B, REMARK 900 ASP 74C AND SER 74D) INSERTED BETWEEN VAL 74 AND ASN 75 REMARK 900 RELATED ID: 1LZ6 RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH EIGHT AMINO ACID RESIDUES (THR 74A, GLY 74B, REMARK 900 ARG 74C, GLY 74D, ASP 74E, SER 74F, PRO 74G AND ALA 74H) INSERTED REMARK 900 BETWEEN VAL 74 AND ASN 75 REMARK 900 RELATED ID: 1LZR RELATED DB: PDB REMARK 900 LYSOZYME (LZ406) COMPLEXED WITH TETRA-ACETYL- CHITOTETRAOSE REMARK 900 RELATED ID: 1LZS RELATED DB: PDB REMARK 900 LYSOZYME (LZ604) COMPLEXED WITH N- ACETYLCHITOSE OLIGOMERS REMARK 900 RELATED ID: 1OP9 RELATED DB: PDB REMARK 900 COMPLEX OF HUMAN LYSOZYME WITH CAMELID VHH HL6 ANTIBODYFRAGMENT REMARK 900 RELATED ID: 1OUA RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT REMARK 900 RELATED ID: 1OUB RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT REMARK 900 RELATED ID: 1OUC RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT REMARK 900 RELATED ID: 1OUD RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT REMARK 900 RELATED ID: 1OUE RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT REMARK 900 RELATED ID: 1OUF RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT REMARK 900 RELATED ID: 1OUG RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT REMARK 900 RELATED ID: 1OUH RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT REMARK 900 RELATED ID: 1OUI RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT REMARK 900 RELATED ID: 1OUJ RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN REMARK 900 LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT REMARK 900 RELATED ID: 1QSW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64CC65A REMARK 900 RELATED ID: 1RE2 RELATED DB: PDB REMARK 900 HUMAN LYSOZYME LABELLED WITH TWO 2',3'- EPOXYPROPYL BETA- GLYCOSIDE REMARK 900 OF N- ACETYLLACTOSAMINE REMARK 900 RELATED ID: 1REM RELATED DB: PDB REMARK 900 HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53 REMARK 900 RELATED ID: 1REX RELATED DB: PDB REMARK 900 NATIVE HUMAN LYSOZYME REMARK 900 RELATED ID: 1REY RELATED DB: PDB REMARK 900 HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX REMARK 900 RELATED ID: 1REZ RELATED DB: PDB REMARK 900 HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX REMARK 900 RELATED ID: 1TAY RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TYR 63 REPLACED BY ALA (Y63A) REMARK 900 RELATED ID: 1TBY RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TYR 63 REPLACED BY LEU (Y63L) REMARK 900 RELATED ID: 1TCY RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TYR 63 REPLACED BY PHE (Y63F) REMARK 900 RELATED ID: 1TDY RELATED DB: PDB REMARK 900 LYSOZYME MUTANT WITH TYR 63 REPLACED BY TRP (Y63W) REMARK 900 RELATED ID: 1UBZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GLU102-MUTANT HUMAN LYSOZYME DOUBLYLABELED REMARK 900 WITH 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE REMARK 900 RELATED ID: 1WQM RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1WQN RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1WQO RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1WQP RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1WQQ RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1WQR RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF REMARK 900 HUMAN LYSOZYME REMARK 900 RELATED ID: 1YAM RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: NULL; EC: 3.2.1.17; REMARK 900 ENGINEERED: YES; MUTATION: I106V REMARK 900 RELATED ID: 1YAN RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: NULL; EC: 3.2.1.17; REMARK 900 ENGINEERED: YES; MUTATION: I23V REMARK 900 RELATED ID: 1YAO RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: NULL; EC: 3.2.1.17; REMARK 900 ENGINEERED: YES; MUTATION: I56V REMARK 900 RELATED ID: 1YAP RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: NULL; EC: 3.2.1.17; REMARK 900 ENGINEERED: YES; MUTATION: I59V REMARK 900 RELATED ID: 1YAQ RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: NULL; EC: 3.2.1.17; REMARK 900 ENGINEERED: YES; MUTATION: I89V REMARK 900 RELATED ID: 207L RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME C77A REMARK 900 RELATED ID: 208L RELATED DB: PDB REMARK 900 MUTANT HUMAN LYSOZYME C77A REMARK 900 RELATED ID: 2BQA RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQB RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQC RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQD RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQE RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQF RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQG RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQH RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQI RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQJ RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQK RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQL RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQM RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQN RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2BQO RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2HEA RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2HEB RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2HEC RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2HED RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2HEE RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2HEF RELATED DB: PDB REMARK 900 CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OFA PROTEIN TO THE REMARK 900 CONFORMATIONAL STABILITY REMARK 900 RELATED ID: 2LHM RELATED DB: PDB REMARK 900 LYSOZYME (APO) (MUTANT WITH GLN 86 REPLACED B ASP AND ALA 92 REMARK 900 REPLACED BY ASP) (Q86D,A92D) REMARK 900 RELATED ID: 2MEA RELATED DB: PDB REMARK 900 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN REMARK 900 LYSOZYMES AT CONSTANT POSITIONS REMARK 900 RELATED ID: 2MEB RELATED DB: PDB REMARK 900 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN REMARK 900 LYSOZYMES AT CONSTANT POSITIONS REMARK 900 RELATED ID: 2MEC RELATED DB: PDB REMARK 900 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN REMARK 900 LYSOZYMES AT CONSTANT POSITIONS REMARK 900 RELATED ID: 2MED RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2MEE RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2MEF RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2MEG RELATED DB: PDB REMARK 900 CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN REMARK 900 LYSOZYMES AT CONSTANT POSITIONS. REMARK 900 RELATED ID: 2MEH RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 2MEI RELATED DB: PDB REMARK 900 CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY REMARK 900 OF HUMAN LYSOZYME REMARK 900 RELATED ID: 3LHM RELATED DB: PDB REMARK 900 LYSOZYME (HOLO) (MUTANT WITH GLN 86 REPLACED BY ASP AND ALA 92 REMARK 900 REPLACED BY ASP) (Q86D,A92D) REMARK 999 REMARK 999 SEQUENCE REMARK 999 VARIANT DESCRIBED IN UNIPROT WITH FTID=VAR_012050 IN P00695 DBREF 1W08 A 1 130 UNP P00695 LYC_HUMAN 19 148 SEQADV 1W08 ASN A 70 UNP P00695 THR 88 VARIANT SEQRES 1 A 130 LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS SEQRES 2 A 130 ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA SEQRES 3 A 130 ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN SEQRES 4 A 130 THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR SEQRES 5 A 130 ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS SEQRES 6 A 130 ASN ASP GLY LYS ASN PRO GLY ALA VAL ASN ALA CYS HIS SEQRES 7 A 130 LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP SEQRES 8 A 130 ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP PRO GLN SEQRES 9 A 130 GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN SEQRES 10 A 130 ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL HET CL A1131 1 HETNAM CL CHLORIDE ION FORMUL 2 CL CL 1- FORMUL 3 HOH *88(H2 O) HELIX 1 1 GLU A 4 LEU A 15 1 12 HELIX 2 2 SER A 24 GLY A 37 1 14 HELIX 3 3 CYS A 81 LEU A 85 5 5 HELIX 4 4 ILE A 89 VAL A 100 1 12 HELIX 5 5 GLN A 104 ALA A 108 5 5 HELIX 6 6 TRP A 109 CYS A 116 1 8 HELIX 7 7 VAL A 121 VAL A 125 5 5 SHEET 1 AA 3 THR A 43 TYR A 45 0 SHEET 2 AA 3 THR A 52 TYR A 54 -1 O ASP A 53 N ASN A 44 SHEET 3 AA 3 ILE A 59 ASN A 60 -1 O ILE A 59 N TYR A 54 SSBOND 1 CYS A 6 CYS A 128 1555 1555 2.01 SSBOND 2 CYS A 30 CYS A 116 1555 1555 2.07 SSBOND 3 CYS A 65 CYS A 81 1555 1555 2.03 SSBOND 4 CYS A 77 CYS A 95 1555 1555 2.03 SITE 1 AC1 3 SER A 61 ARG A 62 HOH A2040 CRYST1 31.117 56.178 62.488 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.032137 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017800 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016003 0.00000 ATOM 1 N LYS A 1 19.534 32.582 38.371 1.00 25.04 N ATOM 2 CA LYS A 1 18.911 32.387 37.062 1.00 25.51 C ATOM 3 C LYS A 1 17.908 33.472 36.753 1.00 27.65 C ATOM 4 O LYS A 1 17.251 33.988 37.643 1.00 29.70 O ATOM 5 CB LYS A 1 18.184 31.056 37.123 1.00 27.48 C ATOM 6 CG LYS A 1 17.069 30.921 36.093 1.00 24.63 C ATOM 7 CD LYS A 1 16.059 29.845 36.488 1.00 20.32 C ATOM 8 CE LYS A 1 14.972 29.702 35.432 1.00 17.75 C ATOM 9 NZ LYS A 1 14.270 28.408 35.603 1.00 22.15 N ATOM 10 N VAL A 2 17.863 33.900 35.497 1.00 28.50 N ATOM 11 CA VAL A 2 16.885 34.898 35.083 1.00 30.21 C ATOM 12 C VAL A 2 15.664 34.300 34.397 1.00 28.35 C ATOM 13 O VAL A 2 15.836 33.831 33.270 1.00 29.66 O ATOM 14 CB VAL A 2 17.581 35.855 34.098 1.00 32.18 C ATOM 15 CG1 VAL A 2 16.605 36.930 33.620 1.00 33.56 C ATOM 16 CG2 VAL A 2 18.793 36.519 34.728 1.00 32.30 C ATOM 17 N PHE A 3 14.455 34.331 34.965 1.00 26.00 N ATOM 18 CA PHE A 3 13.253 33.780 34.319 1.00 23.41 C ATOM 19 C PHE A 3 12.673 34.632 33.194 1.00 24.23 C ATOM 20 O PHE A 3 12.866 35.846 33.153 1.00 26.76 O ATOM 21 CB PHE A 3 12.074 33.612 35.283 1.00 24.94 C ATOM 22 CG PHE A 3 12.279 32.629 36.401 1.00 22.87 C ATOM 23 CD1 PHE A 3 13.114 32.905 37.452 1.00 21.35 C ATOM 24 CD2 PHE A 3 11.577 31.451 36.411 1.00 24.28 C ATOM 25 CE1 PHE A 3 13.279 32.017 38.448 1.00 22.00 C ATOM 26 CE2 PHE A 3 11.748 30.548 37.437 1.00 24.73 C ATOM 27 CZ PHE A 3 12.603 30.826 38.454 1.00 22.98 C ATOM 28 N GLU A 4 11.947 33.998 32.281 1.00 27.31 N ATOM 29 CA GLU A 4 11.236 34.787 31.295 1.00 26.23 C ATOM 30 C GLU A 4 9.969 35.073 32.095 1.00 22.42 C ATOM 31 O GLU A 4 9.419 34.213 32.788 1.00 20.43 O ATOM 32 CB GLU A 4 10.849 34.079 29.985 1.00 30.60 C ATOM 33 CG GLU A 4 11.835 33.050 29.438 1.00 35.34 C ATOM 34 CD GLU A 4 11.382 32.310 28.174 1.00 38.00 C ATOM 35 OE1 GLU A 4 10.961 33.002 27.203 1.00 38.80 O ATOM 36 OE2 GLU A 4 11.458 31.047 28.169 1.00 37.96 O ATOM 37 N ARG A 5 9.438 36.280 31.965 1.00 19.70 N ATOM 38 CA ARG A 5 8.247 36.627 32.723 1.00 24.24 C ATOM 39 C ARG A 5 7.193 35.539 32.993 1.00 24.56 C ATOM 40 O ARG A 5 6.780 35.260 34.121 1.00 26.02 O ATOM 41 CB ARG A 5 7.547 37.691 31.895 1.00 26.66 C ATOM 42 CG ARG A 5 6.414 38.321 32.616 1.00 26.62 C ATOM 43 CD ARG A 5 6.040 39.536 31.854 1.00 27.84 C ATOM 44 NE ARG A 5 5.628 39.304 30.479 1.00 27.08 N ATOM 45 CZ ARG A 5 4.368 39.062 30.147 1.00 27.36 C ATOM 46 NH1 ARG A 5 3.417 38.955 31.070 1.00 26.05 N ATOM 47 NH2 ARG A 5 4.055 38.918 28.869 1.00 27.22 N ATOM 48 N CYS A 6 6.728 34.918 31.916 1.00 26.48 N ATOM 49 CA CYS A 6 5.624 33.952 31.938 1.00 28.20 C ATOM 50 C CYS A 6 6.040 32.603 32.508 1.00 25.73 C ATOM 51 O CYS A 6 5.264 31.897 33.136 1.00 29.19 O ATOM 52 CB CYS A 6 4.960 33.783 30.561 1.00 29.11 C ATOM 53 SG CYS A 6 4.037 35.199 29.871 1.00 31.87 S ATOM 54 N GLU A 7 7.313 32.252 32.329 1.00 26.37 N ATOM 55 CA GLU A 7 7.865 31.062 32.966 1.00 24.94 C ATOM 56 C GLU A 7 7.690 31.154 34.490 1.00 26.96 C ATOM 57 O GLU A 7 7.139 30.248 35.146 1.00 26.30 O ATOM 58 CB GLU A 7 9.329 30.977 32.559 1.00 26.61 C ATOM 59 CG GLU A 7 10.208 29.937 33.247 1.00 27.99 C ATOM 60 CD GLU A 7 11.713 30.074 32.968 1.00 28.02 C ATOM 61 OE1 GLU A 7 12.230 31.205 32.835 1.00 28.20 O ATOM 62 OE2 GLU A 7 12.440 29.057 32.871 1.00 28.07 O ATOM 63 N LEU A 8 8.207 32.252 35.054 1.00 26.16 N ATOM 64 CA LEU A 8 8.020 32.642 36.454 1.00 23.09 C ATOM 65 C LEU A 8 6.568 32.599 36.852 1.00 23.02 C ATOM 66 O LEU A 8 6.162 31.904 37.775 1.00 21.23 O ATOM 67 CB LEU A 8 8.478 34.073 36.744 1.00 22.28 C ATOM 68 CG LEU A 8 8.606 34.477 38.218 1.00 20.69 C ATOM 69 CD1 LEU A 8 9.455 33.447 38.935 1.00 20.17 C ATOM 70 CD2 LEU A 8 9.233 35.826 38.490 1.00 18.44 C ATOM 71 N ALA A 9 5.767 33.360 36.112 1.00 26.73 N ATOM 72 CA ALA A 9 4.369 33.512 36.479 1.00 24.18 C ATOM 73 C ALA A 9 3.770 32.115 36.639 1.00 23.88 C ATOM 74 O ALA A 9 3.127 31.866 37.656 1.00 22.62 O ATOM 75 CB ALA A 9 3.631 34.329 35.493 1.00 23.11 C ATOM 76 N ARG A 10 4.040 31.229 35.689 1.00 23.61 N ATOM 77 CA ARG A 10 3.476 29.892 35.780 1.00 25.94 C ATOM 78 C ARG A 10 4.070 29.003 36.847 1.00 26.40 C ATOM 79 O ARG A 10 3.425 28.124 37.378 1.00 28.07 O ATOM 80 CB ARG A 10 3.755 29.175 34.474 1.00 27.92 C ATOM 81 CG ARG A 10 2.924 29.837 33.414 1.00 30.37 C ATOM 82 CD ARG A 10 2.937 29.013 32.183 1.00 29.37 C ATOM 83 NE ARG A 10 3.985 29.451 31.287 1.00 28.12 N ATOM 84 CZ ARG A 10 3.842 30.295 30.293 1.00 29.04 C ATOM 85 NH1 ARG A 10 2.672 30.875 29.990 1.00 28.87 N ATOM 86 NH2 ARG A 10 4.949 30.509 29.593 1.00 29.08 N ATOM 87 N THR A 11 5.349 29.194 37.101 1.00 25.62 N ATOM 88 CA THR A 11 5.985 28.502 38.185 1.00 25.48 C ATOM 89 C THR A 11 5.429 28.986 39.504 1.00 25.30 C ATOM 90 O THR A 11 5.248 28.235 40.447 1.00 24.32 O ATOM 91 CB THR A 11 7.454 28.882 38.137 1.00 24.27 C ATOM 92 OG1 THR A 11 7.945 28.567 36.832 1.00 24.00 O ATOM 93 CG2 THR A 11 8.271 27.976 38.995 1.00 24.88 C ATOM 94 N LEU A 12 5.179 30.272 39.620 1.00 26.25 N ATOM 95 CA LEU A 12 4.661 30.637 40.913 1.00 26.11 C ATOM 96 C LEU A 12 3.291 29.986 41.012 1.00 26.21 C ATOM 97 O LEU A 12 2.852 29.501 42.068 1.00 24.74 O ATOM 98 CB LEU A 12 4.524 32.126 41.083 1.00 27.56 C ATOM 99 CG LEU A 12 5.791 32.909 40.806 1.00 29.35 C ATOM 100 CD1 LEU A 12 5.455 34.358 40.857 1.00 30.45 C ATOM 101 CD2 LEU A 12 6.707 32.613 41.905 1.00 29.88 C ATOM 102 N LYS A 13 2.624 30.033 39.861 1.00 27.52 N ATOM 103 CA LYS A 13 1.281 29.503 39.714 1.00 26.90 C ATOM 104 C LYS A 13 1.292 28.071 40.270 1.00 27.25 C ATOM 105 O LYS A 13 0.613 27.689 41.207 1.00 25.73 O ATOM 106 CB LYS A 13 0.957 29.577 38.244 1.00 27.48 C ATOM 107 CG LYS A 13 -0.421 29.170 37.847 1.00 28.20 C ATOM 108 CD LYS A 13 -1.477 29.933 38.498 1.00 28.79 C ATOM 109 CE LYS A 13 -2.741 29.064 38.650 1.00 28.85 C ATOM 110 NZ LYS A 13 -3.975 29.488 37.865 1.00 27.91 N ATOM 111 N ARG A 14 2.186 27.260 39.745 1.00 28.04 N ATOM 112 CA ARG A 14 2.333 25.895 40.186 1.00 28.88 C ATOM 113 C ARG A 14 2.680 25.676 41.665 1.00 28.20 C ATOM 114 O ARG A 14 2.475 24.617 42.233 1.00 27.98 O ATOM 115 CB ARG A 14 3.391 25.303 39.263 1.00 30.94 C ATOM 116 CG ARG A 14 2.879 24.963 37.870 1.00 32.69 C ATOM 117 CD ARG A 14 3.712 23.869 37.160 1.00 32.66 C ATOM 118 NE ARG A 14 5.048 24.418 36.996 1.00 32.04 N ATOM 119 CZ ARG A 14 5.379 25.230 36.016 1.00 34.14 C ATOM 120 NH1 ARG A 14 4.490 25.546 35.096 1.00 35.58 N ATOM 121 NH2 ARG A 14 6.598 25.728 35.958 1.00 37.93 N ATOM 122 N LEU A 15 3.187 26.704 42.322 1.00 29.16 N ATOM 123 CA LEU A 15 3.646 26.638 43.692 1.00 27.34 C ATOM 124 C LEU A 15 2.710 27.237 44.741 1.00 26.59 C ATOM 125 O LEU A 15 3.068 27.387 45.908 1.00 29.97 O ATOM 126 CB LEU A 15 4.917 27.485 43.717 1.00 26.12 C ATOM 127 CG LEU A 15 6.170 26.746 43.281 1.00 23.08 C ATOM 128 CD1 LEU A 15 7.191 27.842 43.188 1.00 23.95 C ATOM 129 CD2 LEU A 15 6.646 25.707 44.211 1.00 19.12 C ATOM 130 N GLY A 16 1.523 27.637 44.298 1.00 26.05 N ATOM 131 CA GLY A 16 0.420 28.115 45.113 1.00 26.51 C ATOM 132 C GLY A 16 0.370 29.553 45.573 1.00 26.13 C ATOM 133 O GLY A 16 -0.180 29.739 46.656 1.00 27.88 O ATOM 134 N MET A 17 0.893 30.513 44.808 1.00 26.58 N ATOM 135 CA MET A 17 0.985 31.920 45.200 1.00 26.06 C ATOM 136 C MET A 17 -0.251 32.687 44.776 1.00 27.15 C ATOM 137 O MET A 17 -0.620 33.686 45.410 1.00 27.16 O ATOM 138 CB MET A 17 2.145 32.620 44.501 1.00 27.62 C ATOM 139 CG MET A 17 3.565 32.268 44.903 1.00 27.39 C ATOM 140 SD MET A 17 4.079 32.785 46.536 1.00 27.93 S ATOM 141 CE MET A 17 4.949 34.336 46.126 1.00 28.39 C ATOM 142 N ASP A 18 -0.877 32.261 43.679 1.00 28.18 N ATOM 143 CA ASP A 18 -2.102 32.885 43.196 1.00 28.02 C ATOM 144 C ASP A 18 -3.235 32.789 44.207 1.00 27.58 C ATOM 145 O ASP A 18 -3.759 31.727 44.489 1.00 27.11 O ATOM 146 CB ASP A 18 -2.666 32.252 41.941 1.00 29.50 C ATOM 147 CG ASP A 18 -3.846 33.042 41.394 1.00 30.56 C ATOM 148 OD1 ASP A 18 -3.670 34.250 41.145 1.00 30.81 O ATOM 149 OD2 ASP A 18 -4.989 32.575 41.177 1.00 32.10 O ATOM 150 N GLY A 19 -3.569 33.946 44.755 1.00 25.75 N ATOM 151 CA GLY A 19 -4.592 34.053 45.774 1.00 26.59 C ATOM 152 C GLY A 19 -4.037 33.702 47.138 1.00 24.82 C ATOM 153 O GLY A 19 -4.729 33.765 48.139 1.00 25.73 O ATOM 154 N TYR A 20 -2.766 33.345 47.245 1.00 24.89 N ATOM 155 CA TYR A 20 -2.323 33.088 48.602 1.00 22.49 C ATOM 156 C TYR A 20 -2.357 34.306 49.470 1.00 19.12 C ATOM 157 O TYR A 20 -1.761 35.301 49.200 1.00 21.11 O ATOM 158 CB TYR A 20 -0.999 32.377 48.578 1.00 22.67 C ATOM 159 CG TYR A 20 -0.424 32.160 49.946 1.00 22.28 C ATOM 160 CD1 TYR A 20 -0.446 30.897 50.484 1.00 19.72 C ATOM 161 CD2 TYR A 20 0.190 33.196 50.655 1.00 21.79 C ATOM 162 CE1 TYR A 20 0.092 30.647 51.701 1.00 19.98 C ATOM 163 CE2 TYR A 20 0.750 32.944 51.887 1.00 20.84 C ATOM 164 CZ TYR A 20 0.684 31.670 52.397 1.00 20.43 C ATOM 165 OH TYR A 20 1.213 31.419 53.635 1.00 21.92 O ATOM 166 N ARG A 21 -3.139 34.214 50.521 1.00 23.74 N ATOM 167 CA ARG A 21 -3.427 35.304 51.436 1.00 25.02 C ATOM 168 C ARG A 21 -3.916 36.448 50.594 1.00 24.83 C ATOM 169 O ARG A 21 -3.455 37.565 50.812 1.00 26.19 O ATOM 170 CB ARG A 21 -2.183 35.742 52.198 1.00 26.09 C ATOM 171 CG ARG A 21 -1.791 34.912 53.390 1.00 26.77 C ATOM 172 CD ARG A 21 -2.979 34.264 54.061 1.00 29.73 C ATOM 173 NE ARG A 21 -2.665 33.600 55.329 1.00 32.62 N ATOM 174 CZ ARG A 21 -2.536 32.286 55.550 1.00 36.66 C ATOM 175 NH1 ARG A 21 -2.663 31.339 54.610 1.00 36.63 N ATOM 176 NH2 ARG A 21 -2.261 31.917 56.799 1.00 37.81 N ATOM 177 N GLY A 22 -4.802 36.181 49.641 1.00 21.52 N ATOM 178 CA GLY A 22 -5.355 37.274 48.871 1.00 20.83 C ATOM 179 C GLY A 22 -4.503 37.882 47.766 1.00 21.23 C ATOM 180 O GLY A 22 -5.035 38.644 46.980 1.00 17.88 O ATOM 181 N ILE A 23 -3.222 37.556 47.647 1.00 22.88 N ATOM 182 CA ILE A 23 -2.386 38.160 46.619 1.00 24.36 C ATOM 183 C ILE A 23 -2.391 37.379 45.294 1.00 23.12 C ATOM 184 O ILE A 23 -1.936 36.241 45.205 1.00 21.56 O ATOM 185 CB ILE A 23 -0.970 38.218 47.193 1.00 25.45 C ATOM 186 CG1 ILE A 23 -0.978 38.963 48.522 1.00 27.18 C ATOM 187 CG2 ILE A 23 -0.027 38.820 46.164 1.00 28.50 C ATOM 188 CD1 ILE A 23 0.284 38.778 49.315 1.00 26.95 C ATOM 189 N SER A 24 -2.906 38.031 44.253 1.00 21.28 N ATOM 190 CA SER A 24 -2.884 37.481 42.895 1.00 22.49 C ATOM 191 C SER A 24 -1.493 37.321 42.254 1.00 23.02 C ATOM 192 O SER A 24 -0.502 37.974 42.563 1.00 21.55 O ATOM 193 CB SER A 24 -3.690 38.343 41.904 1.00 19.14 C ATOM 194 OG SER A 24 -3.218 39.680 41.850 1.00 19.55 O ATOM 195 N LEU A 25 -1.490 36.466 41.251 1.00 23.20 N ATOM 196 CA LEU A 25 -0.273 36.193 40.535 1.00 23.60 C ATOM 197 C LEU A 25 0.318 37.494 40.077 1.00 24.66 C ATOM 198 O LEU A 25 1.513 37.726 40.264 1.00 27.15 O ATOM 199 CB LEU A 25 -0.673 35.238 39.448 1.00 24.37 C ATOM 200 CG LEU A 25 0.571 34.804 38.724 1.00 28.15 C ATOM 201 CD1 LEU A 25 1.567 34.025 39.583 1.00 27.61 C ATOM 202 CD2 LEU A 25 0.007 33.957 37.589 1.00 28.51 C ATOM 203 N ALA A 26 -0.535 38.352 39.535 1.00 23.86 N ATOM 204 CA ALA A 26 -0.129 39.620 38.951 1.00 22.64 C ATOM 205 C ALA A 26 0.596 40.510 39.957 1.00 22.79 C ATOM 206 O ALA A 26 1.647 41.092 39.702 1.00 20.21 O ATOM 207 CB ALA A 26 -1.381 40.348 38.376 1.00 21.61 C ATOM 208 N ASN A 27 -0.007 40.690 41.121 1.00 22.45 N ATOM 209 CA ASN A 27 0.778 41.359 42.167 1.00 23.37 C ATOM 210 C ASN A 27 2.210 40.826 42.482 1.00 21.70 C ATOM 211 O ASN A 27 3.175 41.582 42.690 1.00 18.07 O ATOM 212 CB ASN A 27 -0.097 41.365 43.427 1.00 20.65 C ATOM 213 CG ASN A 27 -1.194 42.382 43.321 1.00 16.96 C ATOM 214 OD1 ASN A 27 -0.928 43.560 43.344 1.00 17.83 O ATOM 215 ND2 ASN A 27 -2.424 41.944 43.212 1.00 18.51 N ATOM 216 N TRP A 28 2.314 39.499 42.495 1.00 19.43 N ATOM 217 CA TRP A 28 3.568 38.851 42.844 1.00 20.05 C ATOM 218 C TRP A 28 4.611 39.186 41.761 1.00 20.40 C ATOM 219 O TRP A 28 5.800 39.353 42.040 1.00 19.43 O ATOM 220 CB TRP A 28 3.312 37.333 42.958 1.00 19.59 C ATOM 221 CG TRP A 28 2.723 36.734 44.215 1.00 20.64 C ATOM 222 CD1 TRP A 28 1.582 35.979 44.322 1.00 19.48 C ATOM 223 CD2 TRP A 28 3.251 36.870 45.544 1.00 20.57 C ATOM 224 NE1 TRP A 28 1.386 35.637 45.641 1.00 22.37 N ATOM 225 CE2 TRP A 28 2.389 36.164 46.414 1.00 21.70 C ATOM 226 CE3 TRP A 28 4.362 37.535 46.088 1.00 18.34 C ATOM 227 CZ2 TRP A 28 2.611 36.111 47.795 1.00 20.52 C ATOM 228 CZ3 TRP A 28 4.598 37.447 47.454 1.00 17.11 C ATOM 229 CH2 TRP A 28 3.715 36.749 48.297 1.00 18.44 C ATOM 230 N MET A 29 4.132 39.224 40.519 1.00 21.40 N ATOM 231 CA MET A 29 4.930 39.448 39.344 1.00 22.10 C ATOM 232 C MET A 29 5.375 40.885 39.362 1.00 23.16 C ATOM 233 O MET A 29 6.550 41.184 39.177 1.00 25.23 O ATOM 234 CB MET A 29 4.104 39.104 38.114 1.00 22.73 C ATOM 235 CG MET A 29 3.906 37.611 37.921 1.00 22.71 C ATOM 236 SD MET A 29 5.425 36.637 37.729 1.00 26.37 S ATOM 237 CE MET A 29 5.968 37.227 36.191 1.00 25.33 C ATOM 238 N CYS A 30 4.446 41.802 39.600 1.00 23.31 N ATOM 239 CA CYS A 30 4.858 43.178 39.606 1.00 21.53 C ATOM 240 C CYS A 30 5.930 43.235 40.704 1.00 21.43 C ATOM 241 O CYS A 30 6.984 43.867 40.583 1.00 17.87 O ATOM 242 CB CYS A 30 3.613 44.023 39.866 1.00 22.11 C ATOM 243 SG CYS A 30 3.831 45.803 39.939 1.00 21.22 S ATOM 244 N LEU A 31 5.664 42.574 41.824 1.00 21.94 N ATOM 245 CA LEU A 31 6.622 42.713 42.915 1.00 23.20 C ATOM 246 C LEU A 31 7.932 42.235 42.359 1.00 21.69 C ATOM 247 O LEU A 31 8.928 42.993 42.315 1.00 21.67 O ATOM 248 CB LEU A 31 6.303 42.012 44.237 1.00 23.58 C ATOM 249 CG LEU A 31 7.280 42.338 45.369 1.00 24.46 C ATOM 250 CD1 LEU A 31 7.008 43.581 46.152 1.00 24.73 C ATOM 251 CD2 LEU A 31 7.206 41.054 46.242 1.00 25.40 C ATOM 252 N ALA A 32 7.897 40.991 41.909 1.00 18.33 N ATOM 253 CA ALA A 32 9.155 40.465 41.356 1.00 19.13 C ATOM 254 C ALA A 32 9.896 41.336 40.336 1.00 21.72 C ATOM 255 O ALA A 32 11.102 41.540 40.421 1.00 23.15 O ATOM 256 CB ALA A 32 8.880 39.142 40.735 1.00 18.53 C ATOM 257 N LYS A 33 9.191 41.823 39.322 1.00 23.13 N ATOM 258 CA LYS A 33 9.753 42.810 38.430 1.00 24.30 C ATOM 259 C LYS A 33 10.488 44.023 39.015 1.00 24.20 C ATOM 260 O LYS A 33 11.612 44.409 38.665 1.00 22.74 O ATOM 261 CB LYS A 33 8.599 43.347 37.597 1.00 26.25 C ATOM 262 CG LYS A 33 9.000 44.043 36.291 1.00 25.22 C ATOM 263 CD LYS A 33 9.284 45.514 36.509 1.00 25.84 C ATOM 264 CE LYS A 33 9.911 46.003 35.226 1.00 24.35 C ATOM 265 NZ LYS A 33 9.985 47.448 35.275 1.00 23.29 N ATOM 266 N TRP A 34 9.817 44.707 39.911 1.00 23.61 N ATOM 267 CA TRP A 34 10.494 45.890 40.412 1.00 23.94 C ATOM 268 C TRP A 34 11.653 45.584 41.374 1.00 23.79 C ATOM 269 O TRP A 34 12.684 46.231 41.458 1.00 23.23 O ATOM 270 CB TRP A 34 9.378 46.741 41.029 1.00 23.70 C ATOM 271 CG TRP A 34 8.568 47.328 39.930 1.00 24.61 C ATOM 272 CD1 TRP A 34 7.380 46.894 39.438 1.00 24.94 C ATOM 273 CD2 TRP A 34 8.934 48.466 39.146 1.00 25.13 C ATOM 274 NE1 TRP A 34 6.977 47.710 38.410 1.00 24.85 N ATOM 275 CE2 TRP A 34 7.920 48.678 38.213 1.00 23.90 C ATOM 276 CE3 TRP A 34 10.020 49.335 39.156 1.00 24.88 C ATOM 277 CZ2 TRP A 34 7.960 49.709 37.313 1.00 24.99 C ATOM 278 CZ3 TRP A 34 10.068 50.348 38.252 1.00 26.16 C ATOM 279 CH2 TRP A 34 9.044 50.532 37.344 1.00 25.51 C ATOM 280 N GLU A 35 11.516 44.496 42.107 1.00 26.35 N ATOM 281 CA GLU A 35 12.555 44.126 43.023 1.00 25.46 C ATOM 282 C GLU A 35 13.680 43.404 42.323 1.00 24.69 C ATOM 283 O GLU A 35 14.810 43.611 42.733 1.00 28.49 O ATOM 284 CB GLU A 35 11.983 43.237 44.118 1.00 25.23 C ATOM 285 CG GLU A 35 10.891 43.946 44.871 1.00 25.97 C ATOM 286 CD GLU A 35 11.447 44.836 45.946 1.00 23.96 C ATOM 287 OE1 GLU A 35 12.666 45.001 46.169 1.00 21.29 O ATOM 288 OE2 GLU A 35 10.524 45.354 46.572 1.00 25.82 O ATOM 289 N SER A 36 13.452 42.563 41.324 1.00 24.84 N ATOM 290 CA SER A 36 14.573 41.757 40.821 1.00 23.77 C ATOM 291 C SER A 36 14.817 41.590 39.326 1.00 20.88 C ATOM 292 O SER A 36 15.851 41.125 38.895 1.00 19.39 O ATOM 293 CB SER A 36 14.365 40.346 41.407 1.00 25.17 C ATOM 294 OG SER A 36 13.572 39.479 40.605 1.00 24.53 O ATOM 295 N GLY A 37 13.829 41.912 38.505 1.00 22.30 N ATOM 296 CA GLY A 37 13.877 41.625 37.084 1.00 20.16 C ATOM 297 C GLY A 37 13.851 40.141 36.821 1.00 21.05 C ATOM 298 O GLY A 37 14.350 39.663 35.783 1.00 22.04 O ATOM 299 N TYR A 38 13.283 39.429 37.794 1.00 20.12 N ATOM 300 CA TYR A 38 12.992 38.027 37.621 1.00 17.68 C ATOM 301 C TYR A 38 14.252 37.227 37.735 1.00 19.46 C ATOM 302 O TYR A 38 14.416 36.167 37.132 1.00 24.11 O ATOM 303 CB TYR A 38 12.428 37.855 36.239 1.00 19.31 C ATOM 304 CG TYR A 38 11.165 38.605 36.016 1.00 19.00 C ATOM 305 CD1 TYR A 38 10.245 38.781 37.036 1.00 17.64 C ATOM 306 CD2 TYR A 38 10.907 39.120 34.747 1.00 21.07 C ATOM 307 CE1 TYR A 38 9.078 39.498 36.735 1.00 19.40 C ATOM 308 CE2 TYR A 38 9.731 39.812 34.426 1.00 18.99 C ATOM 309 CZ TYR A 38 8.824 40.003 35.437 1.00 19.90 C ATOM 310 OH TYR A 38 7.714 40.723 35.053 1.00 19.02 O ATOM 311 N ASN A 39 15.149 37.743 38.559 1.00 21.51 N ATOM 312 CA ASN A 39 16.490 37.233 38.703 1.00 20.17 C ATOM 313 C ASN A 39 16.760 36.633 40.060 1.00 20.94 C ATOM 314 O ASN A 39 16.667 37.293 41.068 1.00 20.44 O ATOM 315 CB ASN A 39 17.406 38.405 38.488 1.00 20.79 C ATOM 316 CG ASN A 39 18.831 38.001 38.498 1.00 21.19 C ATOM 317 OD1 ASN A 39 19.174 37.008 39.107 1.00 25.15 O ATOM 318 ND2 ASN A 39 19.674 38.789 37.865 1.00 23.26 N ATOM 319 N THR A 40 17.122 35.361 40.094 1.00 20.82 N ATOM 320 CA THR A 40 17.238 34.816 41.418 1.00 21.32 C ATOM 321 C THR A 40 18.487 35.317 42.093 1.00 23.07 C ATOM 322 O THR A 40 18.614 35.152 43.300 1.00 23.94 O ATOM 323 CB THR A 40 17.312 33.326 41.368 1.00 18.21 C ATOM 324 OG1 THR A 40 18.362 32.909 40.488 1.00 22.92 O ATOM 325 CG2 THR A 40 16.101 32.899 40.673 1.00 19.56 C ATOM 326 N ARG A 41 19.433 35.899 41.378 1.00 23.41 N ATOM 327 CA ARG A 41 20.676 36.166 42.114 1.00 25.27 C ATOM 328 C ARG A 41 20.795 37.639 42.480 1.00 23.07 C ATOM 329 O ARG A 41 21.858 38.071 42.935 1.00 23.24 O ATOM 330 CB ARG A 41 21.965 35.691 41.426 1.00 26.68 C ATOM 331 CG ARG A 41 21.889 34.290 40.884 1.00 29.95 C ATOM 332 CD ARG A 41 23.225 33.732 40.466 1.00 33.79 C ATOM 333 NE ARG A 41 23.290 33.787 39.016 1.00 35.95 N ATOM 334 CZ ARG A 41 24.378 33.674 38.274 1.00 39.85 C ATOM 335 NH1 ARG A 41 25.568 33.491 38.833 1.00 39.00 N ATOM 336 NH2 ARG A 41 24.256 33.749 36.946 1.00 42.95 N ATOM 337 N ALA A 42 19.697 38.371 42.347 1.00 20.21 N ATOM 338 CA ALA A 42 19.749 39.800 42.601 1.00 22.27 C ATOM 339 C ALA A 42 20.054 40.088 44.079 1.00 22.66 C ATOM 340 O ALA A 42 19.477 39.371 44.870 1.00 16.81 O ATOM 341 CB ALA A 42 18.481 40.490 42.088 1.00 18.37 C ATOM 342 N THR A 43 20.982 41.009 44.379 1.00 25.66 N ATOM 343 CA THR A 43 21.288 41.556 45.701 1.00 28.58 C ATOM 344 C THR A 43 21.165 43.091 45.842 1.00 28.43 C ATOM 345 O THR A 43 21.147 43.826 44.852 1.00 29.14 O ATOM 346 CB THR A 43 22.750 41.241 46.046 1.00 30.32 C ATOM 347 OG1 THR A 43 23.597 42.078 45.243 1.00 33.78 O ATOM 348 CG2 THR A 43 23.153 39.862 45.663 1.00 32.51 C ATOM 349 N ASN A 44 21.104 43.567 47.086 1.00 26.99 N ATOM 350 CA ASN A 44 21.063 44.977 47.404 1.00 25.86 C ATOM 351 C ASN A 44 21.478 45.272 48.818 1.00 24.79 C ATOM 352 O ASN A 44 20.948 44.734 49.789 1.00 20.44 O ATOM 353 CB ASN A 44 19.669 45.502 47.243 1.00 29.82 C ATOM 354 CG ASN A 44 19.714 46.880 46.737 1.00 31.00 C ATOM 355 OD1 ASN A 44 19.356 47.781 47.484 1.00 33.97 O ATOM 356 ND2 ASN A 44 20.134 47.036 45.490 1.00 32.54 N ATOM 357 N TYR A 45 22.505 46.102 48.887 1.00 22.60 N ATOM 358 CA TYR A 45 22.941 46.421 50.201 1.00 23.84 C ATOM 359 C TYR A 45 22.120 47.601 50.643 1.00 26.67 C ATOM 360 O TYR A 45 21.974 48.533 49.871 1.00 29.66 O ATOM 361 CB TYR A 45 24.358 46.891 50.079 1.00 21.53 C ATOM 362 CG TYR A 45 24.983 47.385 51.362 1.00 23.60 C ATOM 363 CD1 TYR A 45 25.204 46.550 52.467 1.00 22.91 C ATOM 364 CD2 TYR A 45 25.345 48.721 51.454 1.00 23.97 C ATOM 365 CE1 TYR A 45 25.791 47.032 53.610 1.00 23.68 C ATOM 366 CE2 TYR A 45 25.945 49.221 52.589 1.00 25.18 C ATOM 367 CZ TYR A 45 26.166 48.382 53.675 1.00 25.04 C ATOM 368 OH TYR A 45 26.782 48.970 54.755 1.00 22.72 O ATOM 369 N ASN A 46 21.589 47.560 51.853 1.00 27.37 N ATOM 370 CA ASN A 46 20.910 48.725 52.367 1.00 28.96 C ATOM 371 C ASN A 46 21.808 49.540 53.311 1.00 28.72 C ATOM 372 O ASN A 46 21.889 49.308 54.518 1.00 27.84 O ATOM 373 CB ASN A 46 19.589 48.327 53.020 1.00 32.03 C ATOM 374 CG ASN A 46 18.524 47.966 51.993 1.00 33.41 C ATOM 375 OD1 ASN A 46 18.064 48.835 51.265 1.00 38.13 O ATOM 376 ND2 ASN A 46 18.143 46.697 51.902 1.00 35.78 N ATOM 377 N ALA A 47 22.473 50.522 52.718 1.00 25.93 N ATOM 378 CA ALA A 47 23.415 51.343 53.448 1.00 25.37 C ATOM 379 C ALA A 47 22.907 51.926 54.747 1.00 24.93 C ATOM 380 O ALA A 47 23.704 52.177 55.660 1.00 24.97 O ATOM 381 CB ALA A 47 23.825 52.458 52.567 1.00 25.01 C ATOM 382 N GLY A 48 21.597 52.149 54.771 1.00 23.33 N ATOM 383 CA GLY A 48 20.875 52.679 55.909 1.00 24.05 C ATOM 384 C GLY A 48 21.087 51.938 57.208 1.00 23.54 C ATOM 385 O GLY A 48 21.379 52.582 58.211 1.00 24.69 O ATOM 386 N ASP A 49 20.982 50.619 57.163 1.00 24.08 N ATOM 387 CA ASP A 49 21.133 49.767 58.337 1.00 24.87 C ATOM 388 C ASP A 49 22.066 48.625 58.006 1.00 23.24 C ATOM 389 O ASP A 49 22.217 47.709 58.779 1.00 24.87 O ATOM 390 CB ASP A 49 19.800 49.174 58.816 1.00 24.74 C ATOM 391 CG ASP A 49 19.088 48.375 57.752 1.00 24.14 C ATOM 392 OD1 ASP A 49 19.612 47.917 56.708 1.00 24.17 O ATOM 393 OD2 ASP A 49 17.891 48.135 57.926 1.00 27.77 O ATOM 394 N ARG A 50 22.707 48.648 56.856 1.00 25.16 N ATOM 395 CA ARG A 50 23.677 47.594 56.515 1.00 26.63 C ATOM 396 C ARG A 50 23.046 46.268 56.154 1.00 22.64 C ATOM 397 O ARG A 50 23.671 45.257 56.014 1.00 25.38 O ATOM 398 CB ARG A 50 24.668 47.393 57.670 1.00 27.59 C ATOM 399 CG ARG A 50 25.390 48.667 58.125 1.00 28.10 C ATOM 400 CD ARG A 50 26.154 48.376 59.389 1.00 29.76 C ATOM 401 NE ARG A 50 26.750 49.542 60.019 1.00 29.61 N ATOM 402 CZ ARG A 50 27.996 49.867 59.767 1.00 31.64 C ATOM 403 NH1 ARG A 50 28.710 49.128 58.906 1.00 32.81 N ATOM 404 NH2 ARG A 50 28.517 50.924 60.372 1.00 30.83 N ATOM 405 N SER A 51 21.742 46.235 56.010 1.00 23.68 N ATOM 406 CA SER A 51 21.122 44.983 55.690 1.00 21.48 C ATOM 407 C SER A 51 21.269 44.755 54.199 1.00 20.31 C ATOM 408 O SER A 51 21.678 45.610 53.446 1.00 24.28 O ATOM 409 CB SER A 51 19.651 45.041 56.117 1.00 21.13 C ATOM 410 OG SER A 51 18.906 45.897 55.278 1.00 22.86 O ATOM 411 N THR A 52 20.865 43.577 53.782 1.00 20.45 N ATOM 412 CA THR A 52 21.020 43.115 52.443 1.00 22.87 C ATOM 413 C THR A 52 19.789 42.337 51.984 1.00 24.48 C ATOM 414 O THR A 52 19.338 41.426 52.660 1.00 19.77 O ATOM 415 CB THR A 52 22.267 42.277 52.395 1.00 25.20 C ATOM 416 OG1 THR A 52 23.400 43.119 52.641 1.00 26.27 O ATOM 417 CG2 THR A 52 22.402 41.789 50.965 1.00 26.95 C ATOM 418 N ASP A 53 19.258 42.738 50.831 1.00 24.89 N ATOM 419 CA ASP A 53 18.047 42.159 50.287 1.00 24.41 C ATOM 420 C ASP A 53 18.451 41.110 49.314 1.00 24.70 C ATOM 421 O ASP A 53 19.361 41.375 48.505 1.00 27.24 O ATOM 422 CB ASP A 53 17.226 43.206 49.541 1.00 24.69 C ATOM 423 CG ASP A 53 16.656 44.264 50.486 1.00 25.87 C ATOM 424 OD1 ASP A 53 15.984 44.024 51.542 1.00 24.87 O ATOM 425 OD2 ASP A 53 16.923 45.429 50.156 1.00 22.95 O ATOM 426 N TYR A 54 17.751 39.981 49.382 1.00 25.13 N ATOM 427 CA TYR A 54 18.152 38.808 48.595 1.00 25.48 C ATOM 428 C TYR A 54 17.077 38.227 47.676 1.00 28.09 C ATOM 429 O TYR A 54 15.869 38.093 47.984 1.00 27.85 O ATOM 430 CB TYR A 54 18.629 37.642 49.484 1.00 25.27 C ATOM 431 CG TYR A 54 19.869 37.918 50.321 1.00 25.74 C ATOM 432 CD1 TYR A 54 19.785 38.614 51.483 1.00 24.78 C ATOM 433 CD2 TYR A 54 21.129 37.489 49.930 1.00 26.76 C ATOM 434 CE1 TYR A 54 20.907 38.885 52.208 1.00 26.10 C ATOM 435 CE2 TYR A 54 22.240 37.731 50.664 1.00 24.96 C ATOM 436 CZ TYR A 54 22.134 38.433 51.816 1.00 25.47 C ATOM 437 OH TYR A 54 23.237 38.692 52.593 1.00 24.85 O ATOM 438 N GLY A 55 17.621 37.793 46.544 1.00 28.03 N ATOM 439 CA GLY A 55 16.867 37.095 45.526 1.00 25.01 C ATOM 440 C GLY A 55 15.734 37.766 44.792 1.00 24.37 C ATOM 441 O GLY A 55 15.597 38.966 44.786 1.00 21.00 O ATOM 442 N ILE A 56 14.939 36.922 44.147 1.00 24.64 N ATOM 443 CA ILE A 56 13.873 37.371 43.285 1.00 22.81 C ATOM 444 C ILE A 56 12.830 38.219 44.002 1.00 21.42 C ATOM 445 O ILE A 56 12.212 39.129 43.453 1.00 19.28 O ATOM 446 CB ILE A 56 13.332 36.079 42.745 1.00 23.49 C ATOM 447 CG1 ILE A 56 12.820 36.279 41.325 1.00 26.33 C ATOM 448 CG2 ILE A 56 12.223 35.605 43.618 1.00 25.79 C ATOM 449 CD1 ILE A 56 12.675 34.913 40.636 1.00 25.19 C ATOM 450 N PHE A 57 12.655 37.963 45.290 1.00 22.64 N ATOM 451 CA PHE A 57 11.713 38.845 45.969 1.00 23.67 C ATOM 452 C PHE A 57 12.377 39.858 46.871 1.00 21.91 C ATOM 453 O PHE A 57 11.664 40.523 47.602 1.00 26.02 O ATOM 454 CB PHE A 57 10.676 38.052 46.749 1.00 23.39 C ATOM 455 CG PHE A 57 9.729 37.327 45.860 1.00 18.97 C ATOM 456 CD1 PHE A 57 8.836 38.027 45.069 1.00 20.45 C ATOM 457 CD2 PHE A 57 9.756 35.980 45.810 1.00 18.93 C ATOM 458 CE1 PHE A 57 7.955 37.375 44.239 1.00 19.23 C ATOM 459 CE2 PHE A 57 8.885 35.302 44.993 1.00 18.70 C ATOM 460 CZ PHE A 57 7.992 35.993 44.207 1.00 19.72 C ATOM 461 N GLN A 58 13.684 40.052 46.742 1.00 24.23 N ATOM 462 CA GLN A 58 14.483 40.890 47.645 1.00 25.78 C ATOM 463 C GLN A 58 14.081 40.885 49.130 1.00 24.77 C ATOM 464 O GLN A 58 13.802 41.917 49.760 1.00 26.00 O ATOM 465 CB GLN A 58 14.581 42.303 47.111 1.00 22.86 C ATOM 466 CG GLN A 58 15.253 42.225 45.751 1.00 25.98 C ATOM 467 CD GLN A 58 16.759 42.256 45.877 1.00 24.97 C ATOM 468 OE1 GLN A 58 17.312 43.233 46.384 1.00 25.57 O ATOM 469 NE2 GLN A 58 17.431 41.231 45.408 1.00 21.32 N ATOM 470 N ILE A 59 14.084 39.666 49.638 1.00 21.01 N ATOM 471 CA ILE A 59 13.924 39.466 51.068 1.00 22.49 C ATOM 472 C ILE A 59 15.093 40.042 51.896 1.00 19.44 C ATOM 473 O ILE A 59 16.268 39.735 51.640 1.00 21.11 O ATOM 474 CB ILE A 59 13.924 37.975 51.422 1.00 21.09 C ATOM 475 CG1 ILE A 59 12.989 37.160 50.554 1.00 23.26 C ATOM 476 CG2 ILE A 59 13.587 37.882 52.900 1.00 21.72 C ATOM 477 CD1 ILE A 59 11.521 37.677 50.382 1.00 23.94 C ATOM 478 N ASN A 60 14.741 40.752 52.952 1.00 16.73 N ATOM 479 CA ASN A 60 15.722 41.427 53.775 1.00 16.40 C ATOM 480 C ASN A 60 16.290 40.561 54.892 1.00 16.58 C ATOM 481 O ASN A 60 15.638 39.717 55.542 1.00 16.16 O ATOM 482 CB ASN A 60 15.181 42.788 54.244 1.00 15.90 C ATOM 483 CG ASN A 60 16.154 43.543 55.113 1.00 16.71 C ATOM 484 OD1 ASN A 60 16.248 43.220 56.295 1.00 19.22 O ATOM 485 ND2 ASN A 60 16.907 44.499 54.557 1.00 18.50 N ATOM 486 N SER A 61 17.571 40.811 55.113 1.00 16.83 N ATOM 487 CA SER A 61 18.301 39.980 56.069 1.00 19.07 C ATOM 488 C SER A 61 18.085 40.324 57.527 1.00 18.75 C ATOM 489 O SER A 61 18.354 39.466 58.366 1.00 20.38 O ATOM 490 CB SER A 61 19.822 39.981 55.857 1.00 17.64 C ATOM 491 OG SER A 61 20.379 41.268 55.834 1.00 18.40 O ATOM 492 N ARG A 62 17.613 41.535 57.811 1.00 19.02 N ATOM 493 CA ARG A 62 17.524 41.973 59.203 1.00 19.37 C ATOM 494 C ARG A 62 16.589 41.106 60.048 1.00 20.52 C ATOM 495 O ARG A 62 16.806 40.944 61.257 1.00 20.57 O ATOM 496 CB ARG A 62 17.044 43.413 59.292 1.00 18.04 C ATOM 497 CG ARG A 62 17.122 44.047 60.693 1.00 17.85 C ATOM 498 CD ARG A 62 16.991 45.539 60.611 1.00 16.83 C ATOM 499 NE ARG A 62 16.985 46.152 61.913 1.00 20.13 N ATOM 500 CZ ARG A 62 18.024 46.642 62.577 1.00 22.28 C ATOM 501 NH1 ARG A 62 19.277 46.670 62.094 1.00 22.26 N ATOM 502 NH2 ARG A 62 17.717 47.137 63.771 1.00 23.52 N ATOM 503 N TYR A 63 15.620 40.501 59.354 1.00 20.91 N ATOM 504 CA TYR A 63 14.479 39.836 59.937 1.00 19.53 C ATOM 505 C TYR A 63 14.071 38.545 59.277 1.00 18.99 C ATOM 506 O TYR A 63 13.478 37.672 59.933 1.00 15.63 O ATOM 507 CB TYR A 63 13.308 40.838 59.992 1.00 19.80 C ATOM 508 CG TYR A 63 12.257 40.303 60.922 1.00 21.25 C ATOM 509 CD1 TYR A 63 12.168 40.739 62.244 1.00 21.84 C ATOM 510 CD2 TYR A 63 11.358 39.353 60.473 1.00 19.50 C ATOM 511 CE1 TYR A 63 11.218 40.248 63.103 1.00 19.83 C ATOM 512 CE2 TYR A 63 10.438 38.851 61.320 1.00 22.36 C ATOM 513 CZ TYR A 63 10.407 39.298 62.621 1.00 21.79 C ATOM 514 OH TYR A 63 9.546 38.901 63.601 1.00 24.92 O ATOM 515 N TRP A 64 14.389 38.394 57.994 1.00 24.09 N ATOM 516 CA TRP A 64 13.909 37.189 57.285 1.00 23.30 C ATOM 517 C TRP A 64 14.814 36.026 56.910 1.00 22.92 C ATOM 518 O TRP A 64 14.358 34.919 56.654 1.00 24.64 O ATOM 519 CB TRP A 64 13.172 37.600 56.048 1.00 23.82 C ATOM 520 CG TRP A 64 12.041 38.512 56.302 1.00 23.54 C ATOM 521 CD1 TRP A 64 11.992 39.773 55.890 1.00 22.68 C ATOM 522 CD2 TRP A 64 10.797 38.246 56.950 1.00 23.22 C ATOM 523 NE1 TRP A 64 10.801 40.343 56.251 1.00 23.69 N ATOM 524 CE2 TRP A 64 10.037 39.420 56.902 1.00 23.55 C ATOM 525 CE3 TRP A 64 10.224 37.135 57.558 1.00 24.31 C ATOM 526 CZ2 TRP A 64 8.757 39.524 57.446 1.00 22.81 C ATOM 527 CZ3 TRP A 64 8.954 37.246 58.104 1.00 23.27 C ATOM 528 CH2 TRP A 64 8.242 38.421 58.055 1.00 22.28 C ATOM 529 N CYS A 65 16.116 36.209 56.937 1.00 23.22 N ATOM 530 CA CYS A 65 16.947 35.068 56.627 1.00 25.75 C ATOM 531 C CYS A 65 18.192 35.297 57.453 1.00 26.23 C ATOM 532 O CYS A 65 18.282 36.314 58.103 1.00 30.12 O ATOM 533 CB CYS A 65 17.182 34.961 55.120 1.00 25.98 C ATOM 534 SG CYS A 65 17.902 36.364 54.269 1.00 26.45 S ATOM 535 N ASN A 66 19.141 34.377 57.463 1.00 26.45 N ATOM 536 CA ASN A 66 20.402 34.606 58.139 1.00 23.74 C ATOM 537 C ASN A 66 21.622 34.682 57.238 1.00 21.67 C ATOM 538 O ASN A 66 21.925 33.772 56.449 1.00 20.44 O ATOM 539 CB ASN A 66 20.597 33.456 59.108 1.00 25.69 C ATOM 540 CG ASN A 66 21.917 33.549 59.860 1.00 28.06 C ATOM 541 OD1 ASN A 66 22.639 34.564 59.859 1.00 26.65 O ATOM 542 ND2 ASN A 66 22.234 32.440 60.537 1.00 29.61 N ATOM 543 N ASP A 67 22.329 35.792 57.368 1.00 21.86 N ATOM 544 CA ASP A 67 23.624 35.880 56.684 1.00 24.78 C ATOM 545 C ASP A 67 24.889 36.107 57.529 1.00 23.09 C ATOM 546 O ASP A 67 25.946 36.400 57.000 1.00 24.62 O ATOM 547 CB ASP A 67 23.565 36.949 55.603 1.00 25.58 C ATOM 548 CG ASP A 67 23.648 38.345 56.145 1.00 25.08 C ATOM 549 OD1 ASP A 67 24.189 38.612 57.258 1.00 22.24 O ATOM 550 OD2 ASP A 67 23.184 39.198 55.353 1.00 26.18 O ATOM 551 N GLY A 68 24.814 35.971 58.841 1.00 22.92 N ATOM 552 CA GLY A 68 26.009 35.972 59.650 1.00 23.12 C ATOM 553 C GLY A 68 26.471 37.340 60.092 1.00 24.85 C ATOM 554 O GLY A 68 27.358 37.440 60.896 1.00 27.40 O ATOM 555 N LYS A 69 25.883 38.407 59.590 1.00 26.92 N ATOM 556 CA LYS A 69 26.553 39.668 59.705 1.00 27.12 C ATOM 557 C LYS A 69 26.096 40.316 60.963 1.00 23.31 C ATOM 558 O LYS A 69 26.857 40.348 61.914 1.00 28.49 O ATOM 559 CB LYS A 69 26.329 40.601 58.510 1.00 29.20 C ATOM 560 CG LYS A 69 26.855 40.004 57.229 1.00 31.61 C ATOM 561 CD LYS A 69 27.046 41.028 56.083 1.00 34.02 C ATOM 562 CE LYS A 69 26.244 40.760 54.796 1.00 31.11 C ATOM 563 NZ LYS A 69 26.302 41.973 53.900 1.00 35.15 N ATOM 564 N ASN A 70 24.904 40.865 60.959 1.00 21.67 N ATOM 565 CA ASN A 70 24.364 41.426 62.179 1.00 21.71 C ATOM 566 C ASN A 70 23.891 40.345 63.166 1.00 23.24 C ATOM 567 O ASN A 70 22.948 39.599 62.896 1.00 25.18 O ATOM 568 CB ASN A 70 23.232 42.310 61.757 1.00 21.95 C ATOM 569 CG ASN A 70 22.571 42.997 62.887 1.00 21.67 C ATOM 570 OD1 ASN A 70 22.730 42.716 64.065 1.00 26.25 O ATOM 571 ND2 ASN A 70 21.725 43.924 62.511 1.00 23.79 N ATOM 572 N PRO A 71 24.577 40.304 64.314 1.00 22.99 N ATOM 573 CA PRO A 71 24.400 39.333 65.415 1.00 21.40 C ATOM 574 C PRO A 71 23.122 39.582 66.173 1.00 26.63 C ATOM 575 O PRO A 71 22.784 38.752 67.022 1.00 29.31 O ATOM 576 CB PRO A 71 25.538 39.595 66.388 1.00 19.43 C ATOM 577 CG PRO A 71 26.048 41.026 65.987 1.00 21.52 C ATOM 578 CD PRO A 71 25.580 41.344 64.599 1.00 19.37 C ATOM 579 N GLY A 72 22.416 40.667 65.844 1.00 30.05 N ATOM 580 CA GLY A 72 21.073 40.922 66.347 1.00 28.59 C ATOM 581 C GLY A 72 19.942 40.812 65.333 1.00 29.31 C ATOM 582 O GLY A 72 18.855 41.283 65.665 1.00 31.16 O ATOM 583 N ALA A 73 20.133 40.200 64.163 1.00 27.89 N ATOM 584 CA ALA A 73 19.073 39.998 63.165 1.00 27.21 C ATOM 585 C ALA A 73 18.236 38.759 63.453 1.00 25.33 C ATOM 586 O ALA A 73 18.643 37.932 64.265 1.00 25.76 O ATOM 587 CB ALA A 73 19.680 39.838 61.770 1.00 26.63 C ATOM 588 N VAL A 74 17.092 38.557 62.805 1.00 23.86 N ATOM 589 CA VAL A 74 16.381 37.377 63.255 1.00 21.87 C ATOM 590 C VAL A 74 16.205 36.189 62.320 1.00 19.21 C ATOM 591 O VAL A 74 16.011 35.078 62.795 1.00 24.14 O ATOM 592 CB VAL A 74 14.970 37.799 63.770 1.00 21.81 C ATOM 593 CG1 VAL A 74 14.100 36.584 63.737 1.00 20.60 C ATOM 594 CG2 VAL A 74 15.077 38.423 65.179 1.00 22.42 C ATOM 595 N ASN A 75 16.235 36.287 61.017 1.00 18.40 N ATOM 596 CA ASN A 75 15.938 34.989 60.334 1.00 20.91 C ATOM 597 C ASN A 75 14.571 34.311 60.526 1.00 19.09 C ATOM 598 O ASN A 75 14.407 33.077 60.657 1.00 18.71 O ATOM 599 CB ASN A 75 17.005 33.882 60.569 1.00 18.39 C ATOM 600 CG ASN A 75 16.893 32.723 59.554 1.00 19.36 C ATOM 601 OD1 ASN A 75 16.217 32.775 58.516 1.00 18.35 O ATOM 602 ND2 ASN A 75 17.561 31.624 59.872 1.00 18.36 N ATOM 603 N ALA A 76 13.507 35.089 60.572 1.00 20.55 N ATOM 604 CA ALA A 76 12.189 34.429 60.731 1.00 20.59 C ATOM 605 C ALA A 76 11.872 33.298 59.730 1.00 19.85 C ATOM 606 O ALA A 76 11.095 32.424 60.074 1.00 17.43 O ATOM 607 CB ALA A 76 11.064 35.459 60.658 1.00 22.01 C ATOM 608 N CYS A 77 12.466 33.233 58.536 1.00 20.24 N ATOM 609 CA CYS A 77 12.192 32.139 57.593 1.00 21.22 C ATOM 610 C CYS A 77 13.101 30.927 57.682 1.00 22.53 C ATOM 611 O CYS A 77 13.125 30.019 56.831 1.00 20.74 O ATOM 612 CB CYS A 77 12.434 32.567 56.154 1.00 22.18 C ATOM 613 SG CYS A 77 11.319 33.783 55.507 1.00 24.43 S ATOM 614 N HIS A 78 13.954 31.000 58.690 1.00 26.12 N ATOM 615 CA HIS A 78 14.843 29.893 58.991 1.00 29.54 C ATOM 616 C HIS A 78 15.475 29.209 57.732 1.00 29.69 C ATOM 617 O HIS A 78 15.335 28.024 57.427 1.00 29.85 O ATOM 618 CB HIS A 78 14.065 29.051 60.017 1.00 30.70 C ATOM 619 CG AHIS A 78 14.380 29.535 61.404 0.50 33.99 C ATOM 620 CG BHIS A 78 12.892 28.408 59.333 0.50 30.79 C ATOM 621 ND1AHIS A 78 15.668 29.595 61.894 0.50 36.38 N ATOM 622 ND1BHIS A 78 12.897 27.115 58.857 0.50 27.96 N ATOM 623 CD2AHIS A 78 13.596 30.050 62.382 0.50 34.01 C ATOM 624 CD2BHIS A 78 11.686 28.918 58.975 0.50 31.08 C ATOM 625 CE1AHIS A 78 15.659 30.095 63.117 0.50 33.57 C ATOM 626 CE1BHIS A 78 11.743 26.847 58.272 0.50 28.03 C ATOM 627 NE2AHIS A 78 14.412 30.380 63.439 0.50 32.88 N ATOM 628 NE2BHIS A 78 10.987 27.927 58.325 0.50 29.68 N ATOM 629 N LEU A 79 16.229 30.016 56.997 1.00 27.85 N ATOM 630 CA LEU A 79 17.080 29.564 55.918 1.00 31.04 C ATOM 631 C LEU A 79 18.268 30.509 55.774 1.00 28.11 C ATOM 632 O LEU A 79 18.188 31.709 56.030 1.00 30.11 O ATOM 633 CB LEU A 79 16.343 29.392 54.578 1.00 33.79 C ATOM 634 CG LEU A 79 15.186 30.332 54.258 1.00 35.42 C ATOM 635 CD1 LEU A 79 15.697 31.731 54.302 1.00 35.37 C ATOM 636 CD2 LEU A 79 14.550 30.051 52.906 1.00 35.81 C ATOM 637 N SER A 80 19.415 29.993 55.368 1.00 26.80 N ATOM 638 CA SER A 80 20.502 30.903 55.054 1.00 28.15 C ATOM 639 C SER A 80 20.061 31.883 53.944 1.00 27.39 C ATOM 640 O SER A 80 19.285 31.564 53.043 1.00 31.13 O ATOM 641 CB SER A 80 21.683 30.030 54.674 1.00 27.11 C ATOM 642 OG SER A 80 22.579 30.813 53.924 1.00 27.83 O ATOM 643 N CYS A 81 20.485 33.131 53.941 1.00 27.55 N ATOM 644 CA CYS A 81 20.049 34.019 52.864 1.00 27.72 C ATOM 645 C CYS A 81 20.458 33.411 51.520 1.00 27.15 C ATOM 646 O CYS A 81 19.805 33.519 50.474 1.00 20.70 O ATOM 647 CB CYS A 81 20.630 35.404 53.127 1.00 26.88 C ATOM 648 SG CYS A 81 19.896 36.162 54.615 1.00 27.45 S ATOM 649 N SER A 82 21.580 32.697 51.573 1.00 26.04 N ATOM 650 CA SER A 82 22.058 32.163 50.298 1.00 28.91 C ATOM 651 C SER A 82 20.988 31.237 49.726 1.00 27.55 C ATOM 652 O SER A 82 20.818 31.068 48.523 1.00 29.86 O ATOM 653 CB SER A 82 23.481 31.572 50.352 1.00 27.52 C ATOM 654 OG SER A 82 23.442 30.338 51.006 1.00 27.53 O ATOM 655 N ALA A 83 20.177 30.603 50.548 1.00 28.80 N ATOM 656 CA ALA A 83 19.277 29.756 49.784 1.00 28.44 C ATOM 657 C ALA A 83 18.248 30.603 49.023 1.00 27.38 C ATOM 658 O ALA A 83 17.324 30.095 48.401 1.00 27.01 O ATOM 659 CB ALA A 83 18.580 28.809 50.739 1.00 27.52 C ATOM 660 N LEU A 84 18.385 31.927 49.097 1.00 26.62 N ATOM 661 CA LEU A 84 17.465 32.788 48.365 1.00 26.62 C ATOM 662 C LEU A 84 18.052 33.218 47.021 1.00 26.50 C ATOM 663 O LEU A 84 17.406 33.867 46.202 1.00 29.12 O ATOM 664 CB LEU A 84 17.152 34.009 49.211 1.00 27.92 C ATOM 665 CG LEU A 84 16.304 33.713 50.449 1.00 27.16 C ATOM 666 CD1 LEU A 84 15.950 34.993 51.205 1.00 27.04 C ATOM 667 CD2 LEU A 84 15.009 33.040 50.061 1.00 28.26 C ATOM 668 N LEU A 85 19.317 32.855 46.812 1.00 22.95 N ATOM 669 CA LEU A 85 20.003 33.125 45.558 1.00 24.18 C ATOM 670 C LEU A 85 20.056 31.899 44.652 1.00 25.52 C ATOM 671 O LEU A 85 21.045 31.688 43.954 1.00 27.14 O ATOM 672 CB LEU A 85 21.432 33.585 45.845 1.00 23.16 C ATOM 673 CG LEU A 85 21.488 34.734 46.835 1.00 21.70 C ATOM 674 CD1 LEU A 85 22.921 35.161 47.083 1.00 19.27 C ATOM 675 CD2 LEU A 85 20.707 35.954 46.342 1.00 23.17 C ATOM 676 N GLN A 86 19.071 31.015 44.658 1.00 22.46 N ATOM 677 CA GLN A 86 19.250 29.912 43.755 1.00 22.66 C ATOM 678 C GLN A 86 18.146 29.848 42.735 1.00 19.40 C ATOM 679 O GLN A 86 17.138 30.472 42.786 1.00 18.97 O ATOM 680 CB GLN A 86 19.207 28.623 44.583 1.00 24.24 C ATOM 681 CG AGLN A 86 20.057 28.281 45.777 0.50 22.15 C ATOM 682 CG BGLN A 86 19.556 27.299 43.897 0.50 24.73 C ATOM 683 CD AGLN A 86 21.519 28.581 45.494 0.50 20.86 C ATOM 684 CD BGLN A 86 20.976 27.144 43.401 0.50 22.91 C ATOM 685 OE1AGLN A 86 22.078 28.021 44.549 0.50 23.44 O ATOM 686 OE1BGLN A 86 21.906 27.460 44.124 0.50 22.77 O ATOM 687 NE2AGLN A 86 22.146 29.414 46.308 0.50 16.19 N ATOM 688 NE2BGLN A 86 21.148 26.663 42.179 0.50 21.49 N ATOM 689 N ASP A 87 18.349 28.951 41.811 1.00 23.04 N ATOM 690 CA ASP A 87 17.550 28.857 40.625 1.00 24.10 C ATOM 691 C ASP A 87 16.223 28.285 40.952 1.00 23.15 C ATOM 692 O ASP A 87 15.234 28.736 40.430 1.00 22.90 O ATOM 693 CB ASP A 87 18.249 27.863 39.716 1.00 25.66 C ATOM 694 CG ASP A 87 19.574 28.363 39.234 1.00 25.72 C ATOM 695 OD1 ASP A 87 19.850 29.572 39.128 1.00 29.44 O ATOM 696 OD2 ASP A 87 20.425 27.520 38.956 1.00 28.73 O ATOM 697 N ASN A 88 16.238 27.258 41.776 1.00 23.87 N ATOM 698 CA ASN A 88 14.979 26.740 42.250 1.00 21.49 C ATOM 699 C ASN A 88 14.411 27.725 43.234 1.00 17.36 C ATOM 700 O ASN A 88 15.041 28.121 44.189 1.00 14.92 O ATOM 701 CB ASN A 88 15.298 25.480 43.034 1.00 22.81 C ATOM 702 CG ASN A 88 14.141 25.121 43.897 1.00 24.58 C ATOM 703 OD1 ASN A 88 13.686 25.895 44.741 1.00 29.21 O ATOM 704 ND2 ASN A 88 13.610 23.949 43.637 1.00 26.41 N ATOM 705 N ILE A 89 13.167 28.117 43.087 1.00 19.97 N ATOM 706 CA ILE A 89 12.705 29.172 43.986 1.00 17.62 C ATOM 707 C ILE A 89 11.712 28.741 45.021 1.00 17.44 C ATOM 708 O ILE A 89 10.883 29.456 45.535 1.00 22.87 O ATOM 709 CB ILE A 89 12.142 30.239 43.150 1.00 15.44 C ATOM 710 CG1 ILE A 89 11.118 29.612 42.223 1.00 16.14 C ATOM 711 CG2 ILE A 89 13.298 30.727 42.352 1.00 17.69 C ATOM 712 CD1 ILE A 89 10.145 30.684 41.612 1.00 16.12 C ATOM 713 N ALA A 90 11.790 27.511 45.417 1.00 16.88 N ATOM 714 CA ALA A 90 10.816 27.173 46.420 1.00 18.21 C ATOM 715 C ALA A 90 11.055 27.861 47.756 1.00 19.02 C ATOM 716 O ALA A 90 10.079 28.154 48.459 1.00 19.99 O ATOM 717 CB ALA A 90 10.857 25.640 46.624 1.00 17.69 C ATOM 718 N ASP A 91 12.321 28.035 48.118 1.00 19.40 N ATOM 719 CA ASP A 91 12.600 28.640 49.414 1.00 22.38 C ATOM 720 C ASP A 91 12.191 30.078 49.410 1.00 20.32 C ATOM 721 O ASP A 91 11.472 30.544 50.219 1.00 19.71 O ATOM 722 CB ASP A 91 14.065 28.548 49.794 1.00 24.56 C ATOM 723 CG ASP A 91 14.478 27.143 50.243 1.00 26.57 C ATOM 724 OD1 ASP A 91 13.658 26.307 50.709 1.00 27.65 O ATOM 725 OD2 ASP A 91 15.682 26.834 50.110 1.00 25.00 O ATOM 726 N ALA A 92 12.570 30.773 48.377 1.00 22.15 N ATOM 727 CA ALA A 92 12.148 32.130 48.245 1.00 22.05 C ATOM 728 C ALA A 92 10.692 32.285 48.550 1.00 22.68 C ATOM 729 O ALA A 92 10.262 33.136 49.326 1.00 19.86 O ATOM 730 CB ALA A 92 12.372 32.462 46.788 1.00 23.20 C ATOM 731 N VAL A 93 9.974 31.407 47.863 1.00 23.80 N ATOM 732 CA VAL A 93 8.537 31.534 47.823 1.00 24.43 C ATOM 733 C VAL A 93 7.952 31.229 49.173 1.00 24.10 C ATOM 734 O VAL A 93 7.065 31.926 49.641 1.00 27.04 O ATOM 735 CB VAL A 93 7.945 30.566 46.790 1.00 26.71 C ATOM 736 CG1 VAL A 93 6.479 30.274 47.102 1.00 25.00 C ATOM 737 CG2 VAL A 93 8.116 31.160 45.396 1.00 24.24 C ATOM 738 N ALA A 94 8.449 30.176 49.785 1.00 21.72 N ATOM 739 CA ALA A 94 8.003 29.862 51.115 1.00 21.88 C ATOM 740 C ALA A 94 8.216 31.012 52.045 1.00 21.97 C ATOM 741 O ALA A 94 7.383 31.314 52.891 1.00 21.10 O ATOM 742 CB ALA A 94 8.783 28.715 51.711 1.00 21.27 C ATOM 743 N CYS A 95 9.393 31.601 51.909 1.00 23.28 N ATOM 744 CA CYS A 95 9.736 32.713 52.780 1.00 23.19 C ATOM 745 C CYS A 95 8.826 33.883 52.338 1.00 21.90 C ATOM 746 O CYS A 95 8.368 34.722 53.095 1.00 23.28 O ATOM 747 CB CYS A 95 11.246 32.941 52.658 1.00 22.26 C ATOM 748 SG CYS A 95 11.868 34.333 53.635 1.00 24.88 S ATOM 749 N ALA A 96 8.538 33.957 51.057 1.00 19.80 N ATOM 750 CA ALA A 96 7.650 35.000 50.606 1.00 22.54 C ATOM 751 C ALA A 96 6.240 34.820 51.186 1.00 22.40 C ATOM 752 O ALA A 96 5.493 35.787 51.361 1.00 20.13 O ATOM 753 CB ALA A 96 7.649 35.056 49.087 1.00 21.79 C ATOM 754 N LYS A 97 5.872 33.601 51.547 1.00 23.67 N ATOM 755 CA LYS A 97 4.490 33.426 51.961 1.00 25.52 C ATOM 756 C LYS A 97 4.433 33.841 53.429 1.00 27.02 C ATOM 757 O LYS A 97 3.461 34.403 53.982 1.00 27.55 O ATOM 758 CB LYS A 97 4.038 31.988 51.737 1.00 25.53 C ATOM 759 CG LYS A 97 3.835 31.579 50.275 1.00 25.76 C ATOM 760 CD LYS A 97 3.676 30.097 50.062 1.00 23.85 C ATOM 761 CE LYS A 97 3.481 29.792 48.621 1.00 24.38 C ATOM 762 NZ LYS A 97 3.032 28.385 48.494 1.00 23.71 N ATOM 763 N ARG A 98 5.569 33.561 54.043 1.00 27.06 N ATOM 764 CA ARG A 98 5.648 33.835 55.454 1.00 28.28 C ATOM 765 C ARG A 98 5.580 35.336 55.648 1.00 25.82 C ATOM 766 O ARG A 98 4.833 35.769 56.511 1.00 26.89 O ATOM 767 CB ARG A 98 6.892 33.227 56.063 1.00 30.28 C ATOM 768 CG ARG A 98 7.175 34.001 57.332 1.00 34.44 C ATOM 769 CD ARG A 98 7.018 33.207 58.583 1.00 35.15 C ATOM 770 NE ARG A 98 7.272 33.959 59.822 1.00 39.67 N ATOM 771 CZ ARG A 98 6.594 35.010 60.309 1.00 38.73 C ATOM 772 NH1 ARG A 98 5.537 35.550 59.682 1.00 38.71 N ATOM 773 NH2 ARG A 98 6.994 35.515 61.465 1.00 34.78 N ATOM 774 N VAL A 99 6.309 36.128 54.875 1.00 23.31 N ATOM 775 CA VAL A 99 6.239 37.566 55.024 1.00 21.82 C ATOM 776 C VAL A 99 4.834 38.056 54.765 1.00 21.51 C ATOM 777 O VAL A 99 4.305 38.849 55.519 1.00 18.84 O ATOM 778 CB VAL A 99 7.119 38.222 53.941 1.00 24.32 C ATOM 779 CG1 VAL A 99 6.918 39.706 53.757 1.00 22.10 C ATOM 780 CG2 VAL A 99 8.543 38.006 54.255 1.00 26.62 C ATOM 781 N VAL A 100 4.203 37.624 53.676 1.00 24.02 N ATOM 782 CA VAL A 100 2.825 38.074 53.483 1.00 24.74 C ATOM 783 C VAL A 100 1.906 37.397 54.501 1.00 21.95 C ATOM 784 O VAL A 100 0.699 37.525 54.477 1.00 24.07 O ATOM 785 CB VAL A 100 2.253 37.922 52.054 1.00 24.42 C ATOM 786 CG1 VAL A 100 2.942 38.825 51.072 1.00 27.25 C ATOM 787 CG2 VAL A 100 2.323 36.508 51.570 1.00 23.85 C ATOM 788 N ARG A 101 2.405 36.638 55.450 1.00 24.18 N ATOM 789 CA ARG A 101 1.471 36.093 56.460 1.00 22.86 C ATOM 790 C ARG A 101 1.437 37.174 57.516 1.00 20.51 C ATOM 791 O ARG A 101 0.520 37.238 58.272 1.00 19.64 O ATOM 792 CB ARG A 101 1.808 34.686 57.019 1.00 20.99 C ATOM 793 CG ARG A 101 1.324 33.455 56.242 1.00 21.55 C ATOM 794 CD ARG A 101 1.179 32.055 56.956 1.00 20.09 C ATOM 795 NE ARG A 101 2.530 31.676 57.346 1.00 20.69 N ATOM 796 CZ ARG A 101 3.459 31.134 56.571 1.00 20.09 C ATOM 797 NH1 ARG A 101 3.362 30.782 55.294 1.00 21.95 N ATOM 798 NH2 ARG A 101 4.612 30.948 57.129 1.00 21.05 N ATOM 799 N ASP A 102 2.415 38.062 57.568 1.00 23.46 N ATOM 800 CA ASP A 102 2.292 39.194 58.464 1.00 22.78 C ATOM 801 C ASP A 102 1.085 39.991 58.002 1.00 23.89 C ATOM 802 O ASP A 102 0.670 39.945 56.850 1.00 23.60 O ATOM 803 CB ASP A 102 3.486 40.079 58.279 1.00 21.56 C ATOM 804 CG ASP A 102 4.435 40.031 59.416 1.00 20.86 C ATOM 805 OD1 ASP A 102 4.154 39.404 60.456 1.00 19.83 O ATOM 806 OD2 ASP A 102 5.487 40.690 59.316 1.00 22.21 O ATOM 807 N PRO A 103 0.489 40.737 58.906 1.00 22.39 N ATOM 808 CA PRO A 103 -0.789 41.404 58.640 1.00 23.86 C ATOM 809 C PRO A 103 -0.839 42.463 57.498 1.00 23.31 C ATOM 810 O PRO A 103 -1.817 42.667 56.800 1.00 26.62 O ATOM 811 CB PRO A 103 -1.070 42.079 59.998 1.00 22.63 C ATOM 812 CG PRO A 103 0.260 42.195 60.611 1.00 22.52 C ATOM 813 CD PRO A 103 0.995 40.978 60.258 1.00 22.40 C ATOM 814 N GLN A 104 0.219 43.225 57.365 1.00 21.87 N ATOM 815 CA GLN A 104 0.533 44.120 56.278 1.00 26.57 C ATOM 816 C GLN A 104 0.579 43.378 54.949 1.00 25.85 C ATOM 817 O GLN A 104 0.420 44.013 53.936 1.00 25.98 O ATOM 818 CB GLN A 104 1.897 44.757 56.571 1.00 28.24 C ATOM 819 CG GLN A 104 2.250 45.902 55.712 1.00 31.35 C ATOM 820 CD GLN A 104 3.128 46.966 56.364 1.00 32.03 C ATOM 821 OE1 GLN A 104 3.398 46.974 57.552 1.00 32.13 O ATOM 822 NE2 GLN A 104 3.581 47.900 55.533 1.00 35.14 N ATOM 823 N GLY A 105 0.705 42.064 54.908 1.00 24.75 N ATOM 824 CA GLY A 105 0.794 41.400 53.618 1.00 26.15 C ATOM 825 C GLY A 105 1.855 41.895 52.652 1.00 24.03 C ATOM 826 O GLY A 105 2.969 42.151 53.086 1.00 19.71 O ATOM 827 N ILE A 106 1.519 42.066 51.373 1.00 23.93 N ATOM 828 CA ILE A 106 2.529 42.472 50.404 1.00 24.87 C ATOM 829 C ILE A 106 2.875 43.968 50.501 1.00 27.63 C ATOM 830 O ILE A 106 3.786 44.473 49.830 1.00 28.19 O ATOM 831 CB ILE A 106 2.156 42.013 48.982 1.00 25.92 C ATOM 832 CG1 ILE A 106 3.277 42.285 47.985 1.00 25.36 C ATOM 833 CG2 ILE A 106 0.927 42.708 48.447 1.00 26.02 C ATOM 834 CD1 ILE A 106 3.056 41.679 46.652 1.00 24.50 C ATOM 835 N ARG A 107 2.197 44.679 51.390 1.00 26.78 N ATOM 836 CA ARG A 107 2.472 46.105 51.451 1.00 31.56 C ATOM 837 C ARG A 107 3.741 46.390 52.262 1.00 28.41 C ATOM 838 O ARG A 107 4.189 47.517 52.400 1.00 29.97 O ATOM 839 CB ARG A 107 1.272 46.810 52.082 1.00 36.99 C ATOM 840 CG ARG A 107 -0.014 46.617 51.272 1.00 39.53 C ATOM 841 CD ARG A 107 -1.192 47.401 51.833 1.00 41.64 C ATOM 842 NE ARG A 107 -1.999 48.022 50.772 1.00 44.85 N ATOM 843 CZ ARG A 107 -2.881 47.298 50.065 1.00 47.39 C ATOM 844 NH1 ARG A 107 -3.044 46.002 50.311 1.00 47.22 N ATOM 845 NH2 ARG A 107 -3.627 47.851 49.116 1.00 49.32 N ATOM 846 N ALA A 108 4.323 45.335 52.815 1.00 25.16 N ATOM 847 CA ALA A 108 5.612 45.316 53.495 1.00 23.76 C ATOM 848 C ALA A 108 6.731 45.713 52.538 1.00 23.24 C ATOM 849 O ALA A 108 7.691 46.374 52.909 1.00 25.81 O ATOM 850 CB ALA A 108 5.878 43.906 54.002 1.00 22.42 C ATOM 851 N TRP A 109 6.613 45.284 51.286 1.00 20.39 N ATOM 852 CA TRP A 109 7.513 45.766 50.260 1.00 18.88 C ATOM 853 C TRP A 109 7.136 47.187 49.862 1.00 20.19 C ATOM 854 O TRP A 109 6.018 47.476 49.395 1.00 19.53 O ATOM 855 CB TRP A 109 7.438 44.828 49.040 1.00 18.79 C ATOM 856 CG TRP A 109 8.147 43.576 49.270 1.00 16.04 C ATOM 857 CD1 TRP A 109 9.490 43.395 49.200 1.00 18.51 C ATOM 858 CD2 TRP A 109 7.591 42.315 49.651 1.00 17.83 C ATOM 859 NE1 TRP A 109 9.842 42.100 49.486 1.00 19.13 N ATOM 860 CE2 TRP A 109 8.659 41.407 49.768 1.00 17.46 C ATOM 861 CE3 TRP A 109 6.297 41.853 49.901 1.00 16.81 C ATOM 862 CZ2 TRP A 109 8.429 40.085 50.111 1.00 18.31 C ATOM 863 CZ3 TRP A 109 6.085 40.528 50.243 1.00 16.08 C ATOM 864 CH2 TRP A 109 7.149 39.655 50.339 1.00 14.85 C ATOM 865 N VAL A 110 8.112 48.066 50.015 1.00 21.74 N ATOM 866 CA VAL A 110 7.989 49.445 49.538 1.00 26.00 C ATOM 867 C VAL A 110 7.800 49.621 48.034 1.00 24.34 C ATOM 868 O VAL A 110 6.928 50.333 47.553 1.00 25.69 O ATOM 869 CB VAL A 110 9.233 50.276 49.899 1.00 27.86 C ATOM 870 CG1 VAL A 110 9.496 50.219 51.405 1.00 30.41 C ATOM 871 CG2 VAL A 110 10.427 49.821 49.123 1.00 28.72 C ATOM 872 N ALA A 111 8.652 48.942 47.288 1.00 23.78 N ATOM 873 CA ALA A 111 8.502 48.843 45.851 1.00 24.04 C ATOM 874 C ALA A 111 7.094 48.327 45.563 1.00 24.17 C ATOM 875 O ALA A 111 6.490 48.891 44.673 1.00 22.22 O ATOM 876 CB ALA A 111 9.561 47.947 45.254 1.00 22.73 C ATOM 877 N TRP A 112 6.476 47.389 46.268 1.00 23.83 N ATOM 878 CA TRP A 112 5.077 47.139 45.910 1.00 25.79 C ATOM 879 C TRP A 112 4.127 48.342 46.029 1.00 25.95 C ATOM 880 O TRP A 112 3.317 48.579 45.129 1.00 24.97 O ATOM 881 CB TRP A 112 4.541 45.848 46.591 1.00 26.65 C ATOM 882 CG TRP A 112 3.147 45.526 46.092 1.00 28.05 C ATOM 883 CD1 TRP A 112 2.772 44.757 45.020 1.00 28.86 C ATOM 884 CD2 TRP A 112 1.934 46.033 46.662 1.00 26.53 C ATOM 885 NE1 TRP A 112 1.401 44.764 44.900 1.00 28.67 N ATOM 886 CE2 TRP A 112 0.865 45.561 45.881 1.00 28.03 C ATOM 887 CE3 TRP A 112 1.649 46.874 47.742 1.00 26.83 C ATOM 888 CZ2 TRP A 112 -0.463 45.868 46.169 1.00 28.70 C ATOM 889 CZ3 TRP A 112 0.338 47.183 48.033 1.00 27.96 C ATOM 890 CH2 TRP A 112 -0.705 46.671 47.250 1.00 29.60 C ATOM 891 N ARG A 113 4.187 49.098 47.117 1.00 27.63 N ATOM 892 CA ARG A 113 3.398 50.360 47.181 1.00 31.02 C ATOM 893 C ARG A 113 3.613 51.440 46.099 1.00 28.96 C ATOM 894 O ARG A 113 2.637 51.958 45.558 1.00 32.02 O ATOM 895 CB ARG A 113 3.538 51.035 48.548 1.00 30.16 C ATOM 896 CG ARG A 113 3.513 50.101 49.733 1.00 32.20 C ATOM 897 CD ARG A 113 3.690 50.920 50.969 1.00 36.15 C ATOM 898 NE ARG A 113 3.909 50.244 52.230 1.00 40.49 N ATOM 899 CZ ARG A 113 5.050 50.272 52.897 1.00 43.61 C ATOM 900 NH1 ARG A 113 6.103 50.913 52.407 1.00 44.87 N ATOM 901 NH2 ARG A 113 5.140 49.645 54.063 1.00 44.93 N ATOM 902 N ASN A 114 4.866 51.736 45.767 1.00 26.97 N ATOM 903 CA ASN A 114 5.232 52.710 44.749 1.00 25.91 C ATOM 904 C ASN A 114 5.012 52.228 43.327 1.00 25.98 C ATOM 905 O ASN A 114 4.781 53.066 42.432 1.00 24.35 O ATOM 906 CB ASN A 114 6.714 53.072 44.920 1.00 26.01 C ATOM 907 CG ASN A 114 7.014 53.638 46.311 1.00 27.06 C ATOM 908 OD1 ASN A 114 6.105 54.097 46.997 1.00 26.85 O ATOM 909 ND2 ASN A 114 8.270 53.634 46.737 1.00 24.70 N ATOM 910 N ARG A 115 5.100 50.912 43.116 1.00 25.28 N ATOM 911 CA ARG A 115 5.033 50.416 41.739 1.00 27.07 C ATOM 912 C ARG A 115 3.774 49.666 41.393 1.00 25.89 C ATOM 913 O ARG A 115 3.343 49.724 40.280 1.00 25.96 O ATOM 914 CB ARG A 115 6.213 49.555 41.300 1.00 27.16 C ATOM 915 CG ARG A 115 7.500 50.166 41.758 1.00 30.53 C ATOM 916 CD ARG A 115 7.828 51.411 41.000 1.00 32.57 C ATOM 917 NE ARG A 115 9.080 51.958 41.481 1.00 35.10 N ATOM 918 CZ ARG A 115 9.693 52.967 40.869 1.00 40.34 C ATOM 919 NH1 ARG A 115 9.122 53.493 39.783 1.00 40.14 N ATOM 920 NH2 ARG A 115 10.848 53.458 41.328 1.00 40.45 N ATOM 921 N CYS A 116 3.145 48.984 42.329 1.00 26.82 N ATOM 922 CA CYS A 116 2.007 48.167 41.954 1.00 25.08 C ATOM 923 C CYS A 116 0.684 48.613 42.564 1.00 22.62 C ATOM 924 O CYS A 116 -0.347 48.453 41.956 1.00 23.73 O ATOM 925 CB CYS A 116 2.368 46.777 42.459 1.00 25.60 C ATOM 926 SG CYS A 116 4.019 46.387 41.911 1.00 24.83 S ATOM 927 N GLN A 117 0.666 49.155 43.769 1.00 23.63 N ATOM 928 CA GLN A 117 -0.591 49.500 44.432 1.00 21.23 C ATOM 929 C GLN A 117 -1.327 50.540 43.613 1.00 21.98 C ATOM 930 O GLN A 117 -0.785 51.579 43.301 1.00 24.12 O ATOM 931 CB GLN A 117 -0.264 49.937 45.861 1.00 21.30 C ATOM 932 CG GLN A 117 -1.428 50.103 46.826 1.00 22.99 C ATOM 933 CD GLN A 117 -1.065 51.034 47.975 1.00 22.04 C ATOM 934 OE1 GLN A 117 0.105 51.228 48.285 1.00 20.96 O ATOM 935 NE2 GLN A 117 -2.082 51.605 48.610 1.00 23.48 N ATOM 936 N ASN A 118 -2.552 50.214 43.226 1.00 23.72 N ATOM 937 CA ASN A 118 -3.516 51.069 42.541 1.00 26.76 C ATOM 938 C ASN A 118 -3.060 51.373 41.144 1.00 28.76 C ATOM 939 O ASN A 118 -3.513 52.330 40.555 1.00 28.84 O ATOM 940 CB ASN A 118 -3.850 52.369 43.280 1.00 26.71 C ATOM 941 CG ASN A 118 -4.619 52.097 44.550 1.00 29.83 C ATOM 942 OD1 ASN A 118 -5.597 51.326 44.605 1.00 30.74 O ATOM 943 ND2 ASN A 118 -4.146 52.718 45.623 1.00 30.94 N ATOM 944 N ARG A 119 -2.133 50.551 40.682 1.00 32.85 N ATOM 945 CA ARG A 119 -1.615 50.595 39.334 1.00 34.55 C ATOM 946 C ARG A 119 -1.951 49.350 38.506 1.00 33.98 C ATOM 947 O ARG A 119 -2.613 48.397 38.950 1.00 32.93 O ATOM 948 CB ARG A 119 -0.118 50.820 39.458 1.00 38.94 C ATOM 949 CG ARG A 119 0.279 52.176 40.026 1.00 40.82 C ATOM 950 CD ARG A 119 1.788 52.253 40.039 1.00 43.52 C ATOM 951 NE ARG A 119 2.331 53.400 40.747 1.00 46.45 N ATOM 952 CZ ARG A 119 2.608 54.526 40.133 1.00 47.78 C ATOM 953 NH1 ARG A 119 2.353 54.564 38.837 1.00 47.94 N ATOM 954 NH2 ARG A 119 3.101 55.561 40.802 1.00 49.29 N ATOM 955 N ASP A 120 -1.490 49.414 37.262 1.00 30.86 N ATOM 956 CA ASP A 120 -1.637 48.321 36.303 1.00 30.62 C ATOM 957 C ASP A 120 -0.786 47.048 36.590 1.00 30.40 C ATOM 958 O ASP A 120 0.463 47.014 36.496 1.00 27.94 O ATOM 959 CB ASP A 120 -1.392 48.894 34.880 1.00 28.66 C ATOM 960 CG ASP A 120 -1.392 47.814 33.845 1.00 25.49 C ATOM 961 OD1 ASP A 120 -2.048 46.805 34.151 1.00 25.60 O ATOM 962 OD2 ASP A 120 -0.773 47.856 32.758 1.00 30.59 O ATOM 963 N VAL A 121 -1.442 45.941 36.933 1.00 29.77 N ATOM 964 CA VAL A 121 -0.581 44.777 37.163 1.00 29.53 C ATOM 965 C VAL A 121 -0.826 43.615 36.206 1.00 26.01 C ATOM 966 O VAL A 121 0.084 42.810 36.005 1.00 26.77 O ATOM 967 CB VAL A 121 -0.542 44.485 38.639 1.00 30.39 C ATOM 968 CG1 VAL A 121 -0.275 45.780 39.349 1.00 30.94 C ATOM 969 CG2 VAL A 121 -1.879 44.051 39.074 1.00 31.17 C ATOM 970 N ARG A 122 -1.992 43.616 35.572 1.00 27.10 N ATOM 971 CA ARG A 122 -2.410 42.645 34.576 1.00 27.54 C ATOM 972 C ARG A 122 -1.244 42.495 33.605 1.00 26.42 C ATOM 973 O ARG A 122 -0.822 41.381 33.297 1.00 29.30 O ATOM 974 CB ARG A 122 -3.743 43.011 33.914 1.00 32.53 C ATOM 975 CG ARG A 122 -4.956 43.303 34.840 1.00 38.24 C ATOM 976 CD ARG A 122 -6.438 43.192 34.316 1.00 43.21 C ATOM 977 NE ARG A 122 -7.361 44.313 34.599 1.00 45.84 N ATOM 978 CZ ARG A 122 -8.237 44.449 35.613 1.00 49.00 C ATOM 979 NH1 ARG A 122 -8.395 43.523 36.566 1.00 50.14 N ATOM 980 NH2 ARG A 122 -8.984 45.552 35.714 1.00 47.08 N ATOM 981 N GLN A 123 -0.666 43.615 33.171 1.00 23.26 N ATOM 982 CA GLN A 123 0.422 43.676 32.201 1.00 22.34 C ATOM 983 C GLN A 123 1.498 42.630 32.427 1.00 20.25 C ATOM 984 O GLN A 123 1.951 41.961 31.496 1.00 22.15 O ATOM 985 CB GLN A 123 1.060 45.064 32.217 1.00 23.32 C ATOM 986 CG GLN A 123 1.461 45.553 33.599 1.00 25.01 C ATOM 987 CD GLN A 123 2.113 46.937 33.515 1.00 27.93 C ATOM 988 OE1 GLN A 123 3.008 47.152 32.683 1.00 30.02 O ATOM 989 NE2 GLN A 123 1.678 47.871 34.359 1.00 23.33 N ATOM 990 N TYR A 124 1.853 42.479 33.696 1.00 20.54 N ATOM 991 CA TYR A 124 2.881 41.557 34.127 1.00 22.21 C ATOM 992 C TYR A 124 2.334 40.175 33.954 1.00 22.74 C ATOM 993 O TYR A 124 3.179 39.327 34.167 1.00 22.03 O ATOM 994 CB TYR A 124 3.358 41.712 35.601 1.00 24.40 C ATOM 995 CG TYR A 124 3.830 43.138 35.849 1.00 25.54 C ATOM 996 CD1 TYR A 124 4.980 43.656 35.265 1.00 24.80 C ATOM 997 CD2 TYR A 124 3.052 43.994 36.601 1.00 23.05 C ATOM 998 CE1 TYR A 124 5.353 44.984 35.493 1.00 25.97 C ATOM 999 CE2 TYR A 124 3.399 45.254 36.823 1.00 22.12 C ATOM 1000 CZ TYR A 124 4.539 45.801 36.269 1.00 26.19 C ATOM 1001 OH TYR A 124 4.789 47.157 36.535 1.00 25.62 O ATOM 1002 N VAL A 125 1.043 39.940 33.679 1.00 24.15 N ATOM 1003 CA VAL A 125 0.560 38.570 33.463 1.00 25.32 C ATOM 1004 C VAL A 125 0.020 38.354 32.076 1.00 27.32 C ATOM 1005 O VAL A 125 -0.222 37.198 31.709 1.00 28.49 O ATOM 1006 CB VAL A 125 -0.426 37.999 34.463 1.00 25.43 C ATOM 1007 CG1 VAL A 125 0.280 37.632 35.729 1.00 24.83 C ATOM 1008 CG2 VAL A 125 -1.539 38.959 34.729 1.00 27.16 C ATOM 1009 N GLN A 126 -0.038 39.461 31.341 1.00 28.24 N ATOM 1010 CA GLN A 126 -0.661 39.444 30.035 1.00 28.64 C ATOM 1011 C GLN A 126 0.013 38.393 29.204 1.00 28.16 C ATOM 1012 O GLN A 126 1.219 38.327 29.105 1.00 28.61 O ATOM 1013 CB GLN A 126 -0.583 40.794 29.331 1.00 30.51 C ATOM 1014 CG AGLN A 126 -1.650 41.713 29.880 0.50 30.22 C ATOM 1015 CG BGLN A 126 -1.397 41.951 29.942 0.50 30.86 C ATOM 1016 CD AGLN A 126 -2.973 41.453 29.193 0.50 28.66 C ATOM 1017 CD BGLN A 126 -1.169 43.306 29.267 0.50 29.87 C ATOM 1018 OE1AGLN A 126 -3.403 40.324 29.019 0.50 26.85 O ATOM 1019 OE1BGLN A 126 -1.717 44.314 29.680 0.50 29.39 O ATOM 1020 NE2AGLN A 126 -3.626 42.528 28.802 0.50 30.83 N ATOM 1021 NE2BGLN A 126 -0.363 43.326 28.219 0.50 31.52 N ATOM 1022 N GLY A 127 -0.809 37.555 28.605 1.00 31.20 N ATOM 1023 CA GLY A 127 -0.281 36.571 27.689 1.00 31.48 C ATOM 1024 C GLY A 127 0.294 35.356 28.363 1.00 34.19 C ATOM 1025 O GLY A 127 0.936 34.573 27.674 1.00 35.83 O ATOM 1026 N CYS A 128 0.083 35.179 29.662 1.00 35.15 N ATOM 1027 CA CYS A 128 0.757 34.049 30.280 1.00 35.96 C ATOM 1028 C CYS A 128 -0.325 33.009 30.493 1.00 36.59 C ATOM 1029 O CYS A 128 -0.102 31.804 30.623 1.00 37.04 O ATOM 1030 CB CYS A 128 1.559 34.454 31.525 1.00 34.47 C ATOM 1031 SG CYS A 128 2.684 35.825 31.223 1.00 32.31 S ATOM 1032 N GLY A 129 -1.552 33.494 30.460 1.00 38.63 N ATOM 1033 CA GLY A 129 -2.620 32.534 30.606 1.00 40.00 C ATOM 1034 C GLY A 129 -2.412 31.737 31.873 1.00 42.59 C ATOM 1035 O GLY A 129 -2.240 30.522 31.849 1.00 45.12 O ATOM 1036 N VAL A 130 -2.426 32.426 33.004 1.00 44.34 N ATOM 1037 CA VAL A 130 -2.426 31.753 34.294 1.00 45.28 C ATOM 1038 C VAL A 130 -3.537 32.315 35.164 1.00 44.89 C ATOM 1039 O VAL A 130 -4.509 32.987 34.832 1.00 46.34 O ATOM 1040 CB VAL A 130 -1.132 32.004 35.008 1.00 45.75 C ATOM 1041 CG1 VAL A 130 0.000 31.401 34.225 1.00 45.51 C ATOM 1042 CG2 VAL A 130 -0.978 33.496 35.097 1.00 48.27 C ATOM 1043 OXT VAL A 130 -3.620 32.156 36.371 1.00 46.83 O TER 1044 VAL A 130 HETATM 1045 CL CL A1131 20.816 42.591 58.672 1.00 27.28 CL HETATM 1046 O HOH A2001 13.237 25.320 34.253 1.00 40.07 O HETATM 1047 O HOH A2002 19.312 32.392 33.123 1.00 63.46 O HETATM 1048 O HOH A2003 12.943 28.746 26.533 1.00 43.20 O HETATM 1049 O HOH A2004 10.658 38.182 30.383 1.00 21.46 O HETATM 1050 O HOH A2005 3.392 37.043 25.653 1.00 32.91 O HETATM 1051 O HOH A2006 8.043 35.711 28.916 1.00 18.34 O HETATM 1052 O HOH A2007 14.866 30.642 32.290 1.00 38.27 O HETATM 1053 O HOH A2008 6.281 27.195 32.510 1.00 29.13 O HETATM 1054 O HOH A2009 -1.576 29.300 42.463 1.00 50.61 O HETATM 1055 O HOH A2010 1.396 22.159 41.126 1.00 36.17 O HETATM 1056 O HOH A2011 -2.020 27.787 47.207 1.00 53.31 O HETATM 1057 O HOH A2012 -5.751 30.556 43.881 1.00 57.15 O HETATM 1058 O HOH A2013 -4.252 31.336 51.268 1.00 29.72 O HETATM 1059 O HOH A2014 -4.208 40.456 45.144 1.00 33.14 O HETATM 1060 O HOH A2015 -4.259 41.473 40.213 1.00 29.73 O HETATM 1061 O HOH A2016 -3.529 37.397 38.536 1.00 14.91 O HETATM 1062 O HOH A2017 7.980 30.421 59.208 1.00 38.53 O HETATM 1063 O HOH A2018 12.149 48.071 33.503 1.00 18.43 O HETATM 1064 O HOH A2019 11.063 46.997 48.601 1.00 37.26 O HETATM 1065 O HOH A2020 14.912 45.961 47.341 1.00 50.13 O HETATM 1066 O HOH A2021 8.442 42.453 32.834 1.00 16.30 O HETATM 1067 O HOH A2022 19.593 41.561 38.956 1.00 44.81 O HETATM 1068 O HOH A2023 20.421 31.397 41.111 1.00 24.92 O HETATM 1069 O HOH A2024 22.024 35.348 34.720 1.00 40.89 O HETATM 1070 O HOH A2025 22.290 42.651 41.565 1.00 34.05 O HETATM 1071 O HOH A2026 4.381 45.134 29.843 1.00 39.46 O HETATM 1072 O HOH A2027 17.902 47.223 43.993 1.00 49.60 O HETATM 1073 O HOH A2028 17.210 50.157 46.209 1.00 57.73 O HETATM 1074 O HOH A2029 23.486 47.475 46.263 1.00 24.15 O HETATM 1075 O HOH A2030 20.127 49.983 49.049 1.00 22.02 O HETATM 1076 O HOH A2031 22.895 50.386 47.222 1.00 65.44 O HETATM 1077 O HOH A2032 21.000 52.580 50.585 1.00 30.08 O HETATM 1078 O HOH A2033 20.527 55.200 58.730 1.00 43.90 O HETATM 1079 O HOH A2034 25.572 43.765 57.822 1.00 65.57 O HETATM 1080 O HOH A2035 28.185 47.491 56.691 1.00 30.10 O HETATM 1081 O HOH A2036 23.587 42.342 55.667 1.00 47.93 O HETATM 1082 O HOH A2037 13.687 36.301 47.435 1.00 13.07 O HETATM 1083 O HOH A2038 13.320 44.573 49.438 1.00 30.29 O HETATM 1084 O HOH A2039 11.772 41.579 53.116 1.00 23.27 O HETATM 1085 O HOH A2040 20.411 45.292 59.969 1.00 20.94 O HETATM 1086 O HOH A2041 13.662 44.468 60.139 1.00 29.23 O HETATM 1087 O HOH A2042 18.022 37.754 59.842 1.00 23.04 O HETATM 1088 O HOH A2043 19.742 31.866 62.177 1.00 30.80 O HETATM 1089 O HOH A2044 24.615 31.618 56.892 1.00 57.49 O HETATM 1090 O HOH A2045 21.285 29.696 58.725 1.00 18.42 O HETATM 1091 O HOH A2046 22.419 39.848 58.649 1.00 33.22 O HETATM 1092 O HOH A2047 21.154 37.705 59.176 1.00 23.62 O HETATM 1093 O HOH A2048 28.314 36.902 56.837 1.00 50.33 O HETATM 1094 O HOH A2049 29.536 37.941 59.660 1.00 40.28 O HETATM 1095 O HOH A2050 22.415 37.429 61.281 1.00 36.64 O HETATM 1096 O HOH A2051 18.967 34.709 63.676 1.00 23.33 O HETATM 1097 O HOH A2052 10.724 29.520 54.582 1.00 48.34 O HETATM 1098 O HOH A2053 8.690 30.016 56.482 1.00 38.24 O HETATM 1099 O HOH A2054 14.181 30.722 66.024 1.00 32.56 O HETATM 1100 O HOH A2055 18.983 28.820 58.470 1.00 17.28 O HETATM 1101 O HOH A2056 19.126 27.685 54.562 1.00 24.51 O HETATM 1102 O HOH A2057 22.389 27.702 50.046 1.00 23.42 O HETATM 1103 O HOH A2058 24.194 33.572 53.263 1.00 23.34 O HETATM 1104 O HOH A2059 15.668 34.323 44.671 1.00 27.07 O HETATM 1105 O HOH A2060 25.293 30.482 47.264 1.00 43.88 O HETATM 1106 O HOH A2061 18.503 25.016 42.268 1.00 25.65 O HETATM 1107 O HOH A2062 15.510 31.782 44.852 1.00 26.14 O HETATM 1108 O HOH A2063 12.616 27.227 39.632 1.00 53.04 O HETATM 1109 O HOH A2064 15.001 29.582 46.494 1.00 33.76 O HETATM 1110 O HOH A2065 14.530 26.510 46.782 1.00 23.76 O HETATM 1111 O HOH A2066 11.531 25.948 41.301 1.00 23.58 O HETATM 1112 O HOH A2067 8.115 26.184 48.082 1.00 33.74 O HETATM 1113 O HOH A2068 5.981 29.803 54.173 1.00 51.74 O HETATM 1114 O HOH A2069 1.421 28.430 54.986 1.00 37.95 O HETATM 1115 O HOH A2070 -2.096 39.391 55.458 1.00 21.39 O HETATM 1116 O HOH A2071 -1.946 43.540 52.881 1.00 53.25 O HETATM 1117 O HOH A2072 3.740 41.652 55.620 1.00 25.67 O HETATM 1118 O HOH A2073 -1.330 41.676 50.907 1.00 32.56 O HETATM 1119 O HOH A2074 -4.531 50.305 48.183 1.00 53.80 O HETATM 1120 O HOH A2075 -3.704 43.292 48.058 1.00 38.26 O HETATM 1121 O HOH A2076 11.097 46.995 51.150 1.00 20.95 O HETATM 1122 O HOH A2077 10.447 52.206 45.206 1.00 36.76 O HETATM 1123 O HOH A2078 0.814 53.292 50.658 1.00 46.09 O HETATM 1124 O HOH A2079 -0.670 53.593 45.969 1.00 37.93 O HETATM 1125 O HOH A2080 1.788 55.218 43.904 1.00 31.28 O HETATM 1126 O HOH A2081 -5.668 49.856 38.637 1.00 33.53 O HETATM 1127 O HOH A2082 0.536 51.822 35.994 1.00 45.69 O HETATM 1128 O HOH A2083 -4.244 45.944 37.089 1.00 23.25 O HETATM 1129 O HOH A2084 3.680 42.630 28.857 1.00 80.84 O HETATM 1130 O HOH A2085 -2.700 35.971 31.893 1.00 31.71 O HETATM 1131 O HOH A2086 -4.432 38.431 31.410 1.00 41.85 O HETATM 1132 O HOH A2087 1.634 43.262 26.945 1.00 25.33 O HETATM 1133 O HOH A2088 -2.592 33.405 27.170 1.00 26.54 O CONECT 53 1031 CONECT 243 926 CONECT 534 648 CONECT 613 748 CONECT 648 534 CONECT 748 613 CONECT 926 243 CONECT 1031 53 MASTER 776 0 1 7 3 0 1 6 1119 1 8 10 END If you find results from this site helpful for your research, please cite one of our papers:
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